GRB2

Last updated

GRB2
Grb2.JPG
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GRB2 , ASH, EGFRBP-Grb3-3, MST084, MSTP084, NCKAP2, growth factor receptor bound protein 2
External IDs OMIM: 108355 MGI: 95805 HomoloGene: 1576 GeneCards: GRB2
Orthologs
SpeciesHumanMouse
Entrez

2885

14784

Ensembl

ENSG00000177885

ENSMUSG00000059923

UniProt

P62993

Q60631

RefSeq (mRNA)

NM_203506
NM_002086

NM_008163
NM_001313936
NM_001313937

RefSeq (protein)

NP_002077
NP_987102

NP_001300865
NP_001300866
NP_032189

Location (UCSC) Chr 17: 75.32 – 75.41 Mb Chr 11: 115.53 – 115.6 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Growth factor receptor-bound protein 2, also known as Grb2, is an adaptor protein involved in signal transduction/cell communication. In humans, the GRB2 protein is encoded by the GRB2 gene. [5] [6]

The protein encoded by this gene binds receptors such as the epidermal growth factor receptor and contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. This gene is similar to the sem-5 gene of Caenorhabditis elegans , which is involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene. [7]

Function and expression

Grb2 is widely expressed and is essential for multiple cellular functions. Inhibition of Grb2 function impairs developmental processes in various organisms and blocks transformation and proliferation of various cell types. It is thus not surprising that targeted gene disruption of Grb2 in mice is lethal at an early embryonic stage. Grb2 is best known for its ability to link the epidermal growth factor receptor tyrosine kinase to the activation of Ras and its downstream kinases, ERK1,2. Grb2 is composed of an SH2 domain flanked on each side by an SH3 domain. Grb2 has two closely related proteins with similar domain organizations, Gads and Grap. Gads and Grap are expressed specifically in hematopoietic cells and function in the coordination of tyrosine kinase mediated signal transduction.

Domains

The SH2 domain of Grb2 binds to phosphorylated tyrosine-containing peptides on receptors or scaffold proteins with a preference for pY-X-N-X, where X is generally a hydrophobic residue such as valine (see ).

The N-terminal SH3 domain binds to proline-rich peptides and can bind to the Ras-guanine exchange factor SOS.

The C-terminal SH3 domain binds to peptides conforming to a P-X-I/L/V/-D/N-R-X-X-K-P motif that allows it to specifically bind to proteins such as Gab-1. [8]

Interactions

Grb2 has been shown to interact with:

See also

Related Research Articles

<span class="mw-page-title-main">Epidermal growth factor receptor</span> Transmembrane protein

The epidermal growth factor receptor is a transmembrane protein that is a receptor for members of the epidermal growth factor family of extracellular protein ligands.

<span class="mw-page-title-main">Lck</span> Lymphocyte protein

Lck is a 56 kDa protein that is found inside specialized cells of the immune system called lymphocytes. The Lck is a member of Src kinase family (SFK) and is important for the activation of T-cell receptor (TCR) signaling in both naive T cells and effector T cells. The role of Lck is less prominent in the activation or in the maintenance of memory CD8 T cells in comparison to CD4 T cells. In addition, the constitutive activity of the mouse Lck homolog varies among memory T cell subsets. It seems that in mice, in the effector memory T cell (TEM) population, more than 50% of Lck is present in a constitutively active conformation, whereas less than 20% of Lck is present as active form in central memory T cells. These differences are due to differential regulation by SH2 domain–containing phosphatase-1 (Shp-1) and C-terminal Src kinase.

<span class="mw-page-title-main">Platelet-derived growth factor receptor</span> Cell surface receptors

Platelet-derived growth factor receptors (PDGF-R) are cell surface tyrosine kinase receptors for members of the platelet-derived growth factor (PDGF) family. PDGF subunits -A and -B are important factors regulating cell proliferation, cellular differentiation, cell growth, development and many diseases including cancer. There are two forms of the PDGF-R, alpha and beta each encoded by a different gene. Depending on which growth factor is bound, PDGF-R homo- or heterodimerizes.

<span class="mw-page-title-main">ZAP70</span> Protein-coding gene in the species Homo sapiens

ZAP-70 is a protein normally expressed near the surface membrane of lymphocytes. It is most prominently known to be recruited upon antigen binding to the T cell receptor (TCR), and it plays a critical role in T cell signaling.

<span class="mw-page-title-main">SOS1</span> Protein-coding gene in the species Homo sapiens

Son of sevenless homolog 1 is a protein that in humans is encoded by the SOS1 gene.

<span class="mw-page-title-main">Adapter molecule crk</span> Protein-coding gene in the species Homo sapiens

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.

<span class="mw-page-title-main">Lymphocyte cytosolic protein 2</span> Protein-coding gene in the species Homo sapiens

Lymphocyte cytosolic protein 2, also known as LCP2 or SLP-76, is a signal-transducing adaptor protein expressed in T cells and myeloid cells and is important in the signaling of T-cell receptors (TCRs). As an adaptor protein, SLP-76 does not have catalytic functions, primarily binding other signaling proteins to form larger signaling complexes. It is a key component of the signaling pathways of receptors with immunoreceptor tyrosine-based activation motifs (ITAMs) such as T-cell receptors, its precursors, and receptors for the Fc regions of certain antibodies. SLP-76 is expressed in T-cells and related lymphocytes like natural killer cells.

<span class="mw-page-title-main">Linker for activation of T cells</span> Protein-coding gene in the species Homo sapiens

The Linker for activation of T cells, also known as linker of activated T cells or LAT, is a protein involved in the T-cell antigen receptor signal transduction pathway which in humans is encoded by the LAT gene. Alternative splicing results in multiple transcript variants encoding different isoforms.

<span class="mw-page-title-main">GAB2</span> Protein-coding gene in the species Homo sapiens

GRB2-associated-binding protein 2 also known as GAB2 is a protein that in humans is encoded by the GAB2 gene.

<span class="mw-page-title-main">Janus kinase 2</span> Non-receptor tyrosine kinase and coding gene in humans

Janus kinase 2 is a non-receptor tyrosine kinase. It is a member of the Janus kinase family and has been implicated in signaling by members of the type II cytokine receptor family, the GM-CSF receptor family, the gp130 receptor family, and the single chain receptors.

<span class="mw-page-title-main">PLCG1</span> Protein-coding gene in the species Homo sapiens

Phospholipase C, gamma 1, also known as PLCG1 and PLCgamma1, is a protein that in humans involved in cell growth, migration, apoptosis, and proliferation. It is encoded by the PLCG1 gene and is part of the PLC superfamily.

<span class="mw-page-title-main">CRKL</span> Protein-coding gene in the species Homo sapiens

Crk-like protein is a protein that in humans is encoded by the CRKL gene.

<span class="mw-page-title-main">RAPGEF1</span> Protein-coding gene in the species Homo sapiens

Rap guanine nucleotide exchange factor 1 is a protein that in humans is encoded by the RAPGEF1 gene.

<span class="mw-page-title-main">NCK1</span> Protein-coding gene in the species Homo sapiens

Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.

<span class="mw-page-title-main">INPP5D</span> Protein-coding gene in the species Homo sapiens

Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1(SHIP1) is an enzyme with phosphatase activity. SHIP1 is structured by multiple domain and is encoded by the INPP5D gene in humans. SHIP1 is expressed predominantly by hematopoietic cells but also, for example, by osteoblasts and endothelial cells. This phosphatase is important for the regulation of cellular activation. Not only catalytic but also adaptor activities of this protein are involved in this process. Its movement from the cytosol to the cytoplasmic membrane, where predominantly performs its function, is mediated by tyrosine phosphorylation of the intracellular chains of cell surface receptors that SHIP1 binds. Insufficient regulation of SHIP1 leads to different pathologies.

<span class="mw-page-title-main">PTPRA</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.

<span class="mw-page-title-main">NCK2</span> Protein-coding gene in the species Homo sapiens

Cytoplasmic protein NCK2 is a protein that in humans is encoded by the NCK2 gene.

<span class="mw-page-title-main">GRAP</span> Protein-coding gene in humans

GRB2-related adapter protein is a protein that in humans is encoded by the GRAP gene.

A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases are a subgroup of protein family tyrosine kinases, enzymes that can transfer the phosphate group from ATP to a tyrosine residue of a protein (phosphorylation). These enzymes regulate many cellular functions by switching on or switching off other enzymes in a cell.

Src kinase family is a family of non-receptor tyrosine kinases that includes nine members: Src, Yes, Fyn, and Fgr, forming the SrcA subfamily, Lck, Hck, Blk, and Lyn in the SrcB subfamily, and Frk in its own subfamily. Frk has homologs in invertebrates such as flies and worms, and Src homologs exist in organisms as diverse as unicellular choanoflagellates, but the SrcA and SrcB subfamilies are specific to vertebrates. Src family kinases contain six conserved domains: a N-terminal myristoylated segment, a SH2 domain, a SH3 domain, a linker region, a tyrosine kinase domain, and C-terminal tail.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000177885 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000059923 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Matuoka K, Shibata M, Yamakawa A, Takenawa T (October 1992). "Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries". Proceedings of the National Academy of Sciences of the United States of America. 89 (19): 9015–9. Bibcode:1992PNAS...89.9015M. doi: 10.1073/pnas.89.19.9015 . PMC   50055 . PMID   1384039.
  6. 1 2 Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, Lammers R, Ullrich A, Skolnik EY, Bar-Sagi D, Schlessinger J (August 1992). "The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling". Cell. 70 (3): 431–42. doi: 10.1016/0092-8674(92)90167-B . PMID   1322798.
  7. ↑ "Entrez Gene: GRB2 growth factor receptor-bound protein 2".
  8. ↑ Berry DM, Nash P, Liu SK, Pawson T, McGlade CJ (August 2002). "A high-affinity Arg-X-X-Lys SH3 binding motif confers specificity for the interaction between Gads and SLP-76 in T cell signaling". Current Biology. 12 (15): 1336–41. Bibcode:2002CBio...12.1336B. doi: 10.1016/S0960-9822(02)01038-2 . PMID   12176364. S2CID   15081842.
  9. ↑ Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR (February 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". The Journal of Biological Chemistry. 277 (7): 4999–5007. doi: 10.1074/jbc.M107430200 . PMID   11741929.
  10. ↑ Warmuth M, Bergmann M, Priess A, Häuslmann K, Emmerich B, Hallek M (December 1997). "The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr". The Journal of Biological Chemistry. 272 (52): 33260–70. doi: 10.1074/jbc.272.52.33260 . PMID   9407116.
  11. ↑ Ren R, Ye ZS, Baltimore D (April 1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites". Genes & Development. 8 (7): 783–95. doi: 10.1101/gad.8.7.783 . PMID   7926767.
  12. ↑ VanderNoot VA, Fitzpatrick FA (September 1995). "Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase and growth factor receptor binding protein 2". Analytical Biochemistry. 230 (1): 108–14. doi:10.1006/abio.1995.1444. PMID   8585605.
  13. ↑ Lepley RA, Fitzpatrick FA (September 1994). "5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and cytoskeletal proteins". The Journal of Biological Chemistry. 269 (39): 24163–8. doi: 10.1016/S0021-9258(19)51063-8 . PMID   7929073.
  14. ↑ Fu C, Turck CW, Kurosaki T, Chan AC (July 1998). "BLNK: a central linker protein in B cell activation". Immunity. 9 (1): 93–103. doi: 10.1016/S1074-7613(00)80591-9 . PMID   9697839.
  15. ↑ Engels N, Wollscheid B, Wienands J (July 2001). "Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha". European Journal of Immunology. 31 (7): 2126–34. doi:10.1002/1521-4141(200107)31:7<2126::aid-immu2126>3.0.co;2-o. PMID   11449366. S2CID   31494726.
  16. ↑ Fusaki N, Tomita S, Wu Y, Okamoto N, Goitsuka R, Kitamura D, Hozumi N (May 2000). "BLNK is associated with the CD72/SHP-1/Grb2 complex in the WEHI231 cell line after membrane IgM cross-linking". European Journal of Immunology. 30 (5): 1326–30. doi:10.1002/(sici)1521-4141(200005)30:5<1326::aid-immu1326>3.0.co;2-q. PMID   10820378. S2CID   26610838.
  17. ↑ Wienands J, Schweikert J, Wollscheid B, Jumaa H, Nielsen PJ, Reth M (August 1998). "SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation". The Journal of Experimental Medicine. 188 (4): 791–5. doi:10.1084/jem.188.4.791. PMC   2213353 . PMID   9705962.
  18. 1 2 Angers-Loustau A, Côté JF, Charest A, Dowbenko D, Spencer S, Lasky LA, Tremblay ML (March 1999). "Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts". The Journal of Cell Biology. 144 (5): 1019–31. doi:10.1083/jcb.144.5.1019. PMC   2148201 . PMID   10085298.
  19. ↑ Wang X, Weng LP, Yu Q (May 2000). "Specific inhibition of FGF-induced MAPK activation by the receptor-like protein tyrosine phosphatase LAR". Oncogene. 19 (19): 2346–53. doi:10.1038/sj.onc.1203558. PMID   10822386. S2CID   20434086.
  20. 1 2 3 Million RP, Harakawa N, Roumiantsev S, Varticovski L, Van Etten RA (June 2004). "A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase". Molecular and Cellular Biology. 24 (11): 4685–95. doi:10.1128/MCB.24.11.4685-4695.2004. PMC   416425 . PMID   15143164.
  21. 1 2 3 Puil L, Liu J, Gish G, Mbamalu G, Bowtell D, Pelicci PG, Arlinghaus R, Pawson T (February 1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". The EMBO Journal. 13 (4): 764–73. doi:10.1002/j.1460-2075.1994.tb06319.x. PMC   394874 . PMID   8112292.
  22. ↑ Million RP, Van Etten RA (July 2000). "The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase". Blood. 96 (2): 664–70. doi:10.1182/blood.V96.2.664. PMID   10887132.
  23. ↑ Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene. 17 (8): 941–8. doi:10.1038/sj.onc.1202024. PMID   9747873. S2CID   20866214.
  24. ↑ Ma G, Lu D, Wu Y, Liu J, Arlinghaus RB (May 1997). "Bcr phosphorylated on tyrosine 177 binds Grb2". Oncogene. 14 (19): 2367–72. doi:10.1038/sj.onc.1201053. PMID   9178913. S2CID   9249479.
  25. ↑ Maru Y, Peters KL, Afar DE, Shibuya M, Witte ON, Smithgall TE (February 1995). "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Molecular and Cellular Biology. 15 (2): 835–42. doi:10.1128/mcb.15.2.835. PMC   231961 . PMID   7529874.
  26. ↑ Karoor V, Wang L, Wang HY, Malbon CC (December 1998). "Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350". The Journal of Biological Chemistry. 273 (49): 33035–41. doi: 10.1074/jbc.273.49.33035 . PMID   9830057.
  27. ↑ Ponzetto C, Zhen Z, Audero E, Maina F, Bardelli A, Basile ML, Giordano S, Narsimhan R, Comoglio P (June 1996). "Specific uncoupling of GRB2 from the Met receptor. Differential effects on transformation and motility". The Journal of Biological Chemistry. 271 (24): 14119–23. doi: 10.1074/jbc.271.24.14119 . PMID   8662889.
  28. ↑ Liang Q, Mohan RR, Chen L, Wilson SE (July 1998). "Signaling by HGF and KGF in corneal epithelial cells: Ras/MAP kinase and Jak-STAT pathways". Investigative Ophthalmology & Visual Science. 39 (8): 1329–38. PMID   9660480.
  29. 1 2 Ettenberg SA, Keane MM, Nau MM, Frankel M, Wang LM, Pierce JH, Lipkowitz S (March 1999). "cbl-b inhibits epidermal growth factor receptor signaling". Oncogene. 18 (10): 1855–66. doi: 10.1038/sj.onc.1202499 . PMID   10086340.
  30. ↑ Lavagna-Sévenier C, Marchetto S, Birnbaum D, Rosnet O (June 1998). "The CBL-related protein CBLB participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells". The Journal of Biological Chemistry. 273 (24): 14962–7. doi: 10.1074/jbc.273.24.14962 . PMID   9614102.
  31. ↑ Elly C, Witte S, Zhang Z, Rosnet O, Lipkowitz S, Altman A, Liu YC (February 1999). "Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation". Oncogene. 18 (5): 1147–56. doi:10.1038/sj.onc.1202411. PMID   10022120. S2CID   25964785.
  32. 1 2 Feng GS, Ouyang YB, Hu DP, Shi ZQ, Gentz R, Ni J (May 1996). "Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway". The Journal of Biological Chemistry. 271 (21): 12129–32. doi: 10.1074/jbc.271.21.12129 . PMID   8647802.
  33. ↑ De Sepulveda P, Okkenhaug K, Rose JL, Hawley RG, Dubreuil P, Rottapel R (February 1999). "Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation". The EMBO Journal. 18 (4): 904–15. doi:10.1093/emboj/18.4.904. PMC   1171183 . PMID   10022833.
  34. ↑ Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L (July 1999). "Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor". The Biochemical Journal. 341 (1): 211–6. doi:10.1042/0264-6021:3410211. PMC   1220349 . PMID   10377264.
  35. ↑ Poe JC, Fujimoto M, Jansen PJ, Miller AS, Tedder TF (June 2000). "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux". The Journal of Biological Chemistry. 275 (23): 17420–7. doi: 10.1074/jbc.M001892200 . PMID   10748054.
  36. ↑ Otipoby KL, Draves KE, Clark EA (November 2001). "CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1". The Journal of Biological Chemistry. 276 (47): 44315–22. doi: 10.1074/jbc.M105446200 . PMID   11551923.
  37. ↑ Okkenhaug K, Rottapel R (August 1998). "Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction". The Journal of Biological Chemistry. 273 (33): 21194–202. doi: 10.1074/jbc.273.33.21194 . PMID   9694876.
  38. ↑ Nunès JA, Truneh A, Olive D, Cantrell DA (January 1996). "Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules". The Journal of Biological Chemistry. 271 (3): 1591–8. doi: 10.1074/jbc.271.3.1591 . PMID   8576157.
  39. ↑ Sugiyama Y, Tomoda K, Tanaka T, Arata Y, Yoneda-Kato N, Kato J (April 2001). "Direct binding of the signal-transducing adaptor Grb2 facilitates down-regulation of the cyclin-dependent kinase inhibitor p27Kip1". The Journal of Biological Chemistry. 276 (15): 12084–90. doi: 10.1074/jbc.M010811200 . PMID   11278754.
  40. ↑ Riordan SM, Lidder S, Williams R, Skouteris GG (September 2000). "The beta-subunit of the hepatocyte growth factor/scatter factor (HGF/SF) receptor phosphorylates and associates with CrkII: expression of CrkII enhances HGF/SF-induced mitogenesis". The Biochemical Journal. 350 (3): 925–32. doi:10.1042/0264-6021:3500925. PMC   1221328 . PMID   10970810.
  41. ↑ Matsuda M, Ota S, Tanimura R, Nakamura H, Matuoka K, Takenawa T, Nagashima K, Kurata T (June 1996). "Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins". The Journal of Biological Chemistry. 271 (24): 14468–72. doi: 10.1074/jbc.271.24.14468 . PMID   8662907.
  42. 1 2 Okada S, Pessin JE (October 1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". The Journal of Biological Chemistry. 271 (41): 25533–8. doi: 10.1074/jbc.271.41.25533 . PMID   8810325.
  43. 1 2 Erdreich-Epstein A, Liu M, Kant AM, Izadi KD, Nolta JA, Durden DL (April 1999). "Cbl functions downstream of Src kinases in Fc gamma RI signaling in primary human macrophages". Journal of Leukocyte Biology. 65 (4): 523–34. doi:10.1002/jlb.65.4.523. PMID   10204582. S2CID   18340540.
  44. 1 2 3 Wong A, Lamothe B, Lee A, Schlessinger J, Lax I, Li A (May 2002). "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl". Proceedings of the National Academy of Sciences of the United States of America. 99 (10): 6684–9. Bibcode:2002PNAS...99.6684W. doi: 10.1073/pnas.052138899 . PMC   124463 . PMID   11997436.
  45. 1 2 3 4 5 6 Saci A, Liu WQ, Vidal M, Garbay C, Rendu F, Bachelot-Loza C (May 2002). "Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement". The Biochemical Journal. 363 (Pt 3): 717–25. doi:10.1042/0264-6021:3630717. PMC   1222524 . PMID   11964172.
  46. 1 2 3 Liu SK, McGlade CJ (December 1998). "Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc". Oncogene. 17 (24): 3073–82. doi:10.1038/sj.onc.1202337. PMID   9872323. S2CID   6140122.
  47. 1 2 3 Park RK, Erdreich-Epstein A, Liu M, Izadi KD, Durden DL (December 1999). "High affinity IgG receptor activation of Src family kinases is required for modulation of the Shc-Grb2-Sos complex and the downstream activation of the nicotinamide adenine dinucleotide phosphate (reduced) oxidase". Journal of Immunology. 163 (11): 6023–34. doi: 10.4049/jimmunol.163.11.6023 . PMID   10570290. S2CID   36719981.
  48. ↑ Jain SK, Langdon WY, Varticovski L (May 1997). "Tyrosine phosphorylation of p120cbl in BCR/abl transformed hematopoietic cells mediates enhanced association with phosphatidylinositol 3-kinase". Oncogene. 14 (18): 2217–28. doi: 10.1038/sj.onc.1201049 . PMID   9174058.
  49. ↑ Robertson H, Langdon WY, Thien CB, Bowtell DD (November 1997). "A c-Cbl yeast two hybrid screen reveals interactions with 14-3-3 isoforms and cytoskeletal components". Biochemical and Biophysical Research Communications. 240 (1): 46–50. doi:10.1006/bbrc.1997.7608. PMID   9367879.
  50. ↑ Donovan JA, Wange RL, Langdon WY, Samelson LE (September 1994). "The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor". The Journal of Biological Chemistry. 269 (37): 22921–4. doi: 10.1016/S0021-9258(17)31595-8 . PMID   8083187.
  51. ↑ Gesbert F, Garbay C, Bertoglio J (February 1998). "Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells". The Journal of Biological Chemistry. 273 (7): 3986–93. doi: 10.1074/jbc.273.7.3986 . PMID   9461587.
  52. ↑ Husson H, Mograbi B, Schmid-Antomarchi H, Fischer S, Rossi B (May 1997). "CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2". Oncogene. 14 (19): 2331–8. doi:10.1038/sj.onc.1201074. PMID   9178909. S2CID   967748.
  53. ↑ Odai H, Sasaki K, Iwamatsu A, Nakamoto T, Ueno H, Yamagata T, Mitani K, Yazaki Y, Hirai H (April 1997). "Purification and molecular cloning of SH2- and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl". Blood. 89 (8): 2745–56. doi: 10.1182/blood.V89.8.2745 . PMID   9108392.
  54. ↑ Ng C, Jackson RA, Buschdorf JP, Sun Q, Guy GR, Sivaraman J (March 2008). "Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates". The EMBO Journal. 27 (5): 804–16. doi:10.1038/emboj.2008.18. PMC   2265755 . PMID   18273061.
  55. ↑ Mancini A, Niedenthal R, Joos H, Koch A, Trouliaris S, Niemann H, Tamura T (September 1997). "Identification of a second Grb2 binding site in the v-Fms tyrosine kinase". Oncogene. 15 (13): 1565–72. doi:10.1038/sj.onc.1201518. PMID   9380408. S2CID   7880476.
  56. ↑ Sahni M, Zhou XM, Bakiri L, Schlessinger J, Baron R, Levy JB (December 1996). "Identification of a novel 135-kDa Grb2-binding protein in osteoclasts". The Journal of Biological Chemistry. 271 (51): 33141–7. doi: 10.1074/jbc.271.51.33141 . PMID   8955163.
  57. ↑ Miki H, Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T (February 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". The Journal of Biological Chemistry. 269 (8): 5489–92. doi: 10.1016/S0021-9258(17)37484-7 . PMID   8119878.
  58. 1 2 Sastry L, Cao T, King CR (January 1997). "Multiple Grb2-protein complexes in human cancer cells". International Journal of Cancer. 70 (2): 208–13. doi: 10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e . PMID   9009162. S2CID   10317185.
  59. ↑ Hsia DA, Mitra SK, Hauck CR, Streblow DN, Nelson JA, Ilic D, Huang S, Li E, Nemerow GR, Leng J, Spencer KS, Cheresh DA, Schlaepfer DD (March 2003). "Differential regulation of cell motility and invasion by FAK". The Journal of Cell Biology. 160 (5): 753–67. doi:10.1083/jcb.200212114. PMC   2173366 . PMID   12615911.
  60. ↑ Hasegawa H, Kiyokawa E, Tanaka S, Nagashima K, Gotoh N, Shibuya M, Kurata T, Matsuda M (April 1996). "DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane". Molecular and Cellular Biology. 16 (4): 1770–6. doi:10.1128/mcb.16.4.1770. PMC   231163 . PMID   8657152.
  61. ↑ Yang B, Jung D, Motto D, Meyer J, Koretzky G, Campbell KP (May 1995). "SH3 domain-mediated interaction of dystroglycan and Grb2". The Journal of Biological Chemistry. 270 (20): 11711–4. doi: 10.1074/jbc.270.20.11711 . PMID   7744812.
  62. ↑ Pratt RL, Kinch MS (October 2002). "Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade". Oncogene. 21 (50): 7690–9. doi:10.1038/sj.onc.1205758. PMID   12400011. S2CID   7083192.
  63. 1 2 3 4 Oneyama C, Nakano H, Sharma SV (March 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene. 21 (13): 2037–50. doi:10.1038/sj.onc.1205271. PMID   11960376. S2CID   23869665.
  64. 1 2 3 4 5 Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M (March 2003). "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nature Biotechnology. 21 (3): 315–8. doi:10.1038/nbt790. PMID   12577067. S2CID   26838266.
  65. 1 2 Schulze WX, Deng L, Mann M (2005). "Phosphotyrosine interactome of the ErbB-receptor kinase family". Molecular Systems Biology. 1: E1–E13. doi:10.1038/msb4100012. PMC   1681463 . PMID   16729043.
  66. ↑ Wong L, Deb TB, Thompson SA, Wells A, Johnson GR (March 1999). "A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling". The Journal of Biological Chemistry. 274 (13): 8900–9. doi: 10.1074/jbc.274.13.8900 . PMID   10085134.
  67. ↑ Okutani T, Okabayashi Y, Kido Y, Sugimoto Y, Sakaguchi K, Matuoka K, Takenawa T, Kasuga M (December 1994). "Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells". The Journal of Biological Chemistry. 269 (49): 31310–4. doi: 10.1016/S0021-9258(18)47424-8 . hdl: 20.500.14094/D2001922 . PMID   7527043.
  68. 1 2 Tortora G, Damiano V, Bianco C, Baldassarre G, Bianco AR, Lanfrancone L, Pelicci PG, Ciardiello F (February 1997). "The RIalpha subunit of protein kinase A (PKA) binds to Grb2 and allows PKA interaction with the activated EGF-receptor". Oncogene. 14 (8): 923–8. doi:10.1038/sj.onc.1200906. PMID   9050991. S2CID   10640461.
  69. ↑ Daly RJ, Sanderson GM, Janes PW, Sutherland RL (May 1996). "Cloning and characterization of GRB14, a novel member of the GRB7 gene family". The Journal of Biological Chemistry. 271 (21): 12502–10. doi: 10.1074/jbc.271.21.12502 . PMID   8647858.
  70. 1 2 Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J (March 1994). "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells". The Journal of Biological Chemistry. 269 (12): 9019–23. doi: 10.1016/S0021-9258(17)37070-9 . PMID   7510700.
  71. 1 2 Braverman LE, Quilliam LA (February 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". The Journal of Biological Chemistry. 274 (9): 5542–9. doi: 10.1074/jbc.274.9.5542 . PMID   10026169.
  72. ↑ Tauchi T, Feng GS, Shen R, Hoatlin M, Bagby GC, Kabat D, Lu L, Broxmeyer HE (March 1995). "Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways". The Journal of Biological Chemistry. 270 (10): 5631–5. doi: 10.1074/jbc.270.10.5631 . PMID   7534299.
  73. ↑ Ong SH, Goh KC, Lim YP, Low BC, Klint P, Claesson-Welsh L, Cao X, Tan YH, Guy GR (August 1996). "Suc1-associated neurotrophic factor target (SNT) protein is a major FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to the SH2 domain of GRB2". Biochemical and Biophysical Research Communications. 225 (3): 1021–6. doi:10.1006/bbrc.1996.1288. PMID   8780727.
  74. ↑ Meakin SO, MacDonald JI, Gryz EA, Kubu CJ, Verdi JM (April 1999). "The signaling adapter FRS-2 competes with Shc for binding to the nerve growth factor receptor TrkA. A model for discriminating proliferation and differentiation". The Journal of Biological Chemistry. 274 (14): 9861–70. doi: 10.1074/jbc.274.14.9861 . PMID   10092678.
  75. ↑ Kouhara H, Hadari YR, Spivak-Kroizman T, Schilling J, Bar-Sagi D, Lax I, Schlessinger J (May 1997). "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway". Cell. 89 (5): 693–702. doi: 10.1016/s0092-8674(00)80252-4 . PMID   9182757. S2CID   2187363.
  76. ↑ Ghadimi MP, Sanzenbacher R, Thiede B, Wenzel J, Jing Q, Plomann M, Borkhardt A, Kabelitz D, Janssen O (May 2002). "Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178)". FEBS Letters. 519 (1–3): 50–8. doi:10.1016/s0014-5793(02)02709-6. PMID   12023017. S2CID   26765451.
  77. ↑ Wenzel J, Sanzenbacher R, Ghadimi M, Lewitzky M, Zhou Q, Kaplan DR, Kabelitz D, Feller SM, Janssen O (December 2001). "Multiple interactions of the cytosolic polyproline region of the CD95 ligand: hints for the reverse signal transduction capacity of a death factor". FEBS Letters. 509 (2): 255–62. doi:10.1016/s0014-5793(01)03174-x. PMID   11741599. S2CID   33084576.
  78. 1 2 Lewitzky M, Kardinal C, Gehring NH, Schmidt EK, Konkol B, Eulitz M, Birchmeier W, Schaeper U, Feller SM (March 2001). "The C-terminal SH3 domain of the adapter protein Grb2 binds with high affinity to sequences in Gab1 and SLP-76 which lack the SH3-typical P-x-x-P core motif". Oncogene. 20 (9): 1052–62. doi: 10.1038/sj.onc.1204202 . PMID   11314042.
  79. ↑ Holgado-Madruga M, Emlet DR, Moscatello DK, Godwin AK, Wong AJ (February 1996). "A Grb2-associated docking protein in EGF- and insulin-receptor signalling". Nature. 379 (6565): 560–4. Bibcode:1996Natur.379..560H. doi:10.1038/379560a0. PMID   8596638. S2CID   4271970.
  80. ↑ Lynch DK, Daly RJ (January 2002). "PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2". The EMBO Journal. 21 (1–2): 72–82. doi:10.1093/emboj/21.1.72. PMC   125816 . PMID   11782427.
  81. ↑ Zhao C, Yu DH, Shen R, Feng GS (July 1999). "Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1". The Journal of Biological Chemistry. 274 (28): 19649–54. doi: 10.1074/jbc.274.28.19649 . PMID   10391903.
  82. 1 2 Lee IS, Liu Y, Narazaki M, Hibi M, Kishimoto T, Taga T (January 1997). "Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6". FEBS Letters. 401 (2–3): 133–7. doi: 10.1016/s0014-5793(96)01456-1 . PMID   9013873. S2CID   32632406.
  83. 1 2 Ward AC, Monkhouse JL, Hamilton JA, Csar XF (November 1998). "Direct binding of Shc, Grb2, SHP-2 and p40 to the murine granulocyte colony-stimulating factor receptor". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1448 (1): 70–6. doi: 10.1016/s0167-4889(98)00120-7 . hdl: 10536/DRO/DU:30096477 . PMID   9824671.
  84. 1 2 Bourguignon LY, Zhu H, Zhou B, Diedrich F, Singleton PA, Hung MC (December 2001). "Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth". The Journal of Biological Chemistry. 276 (52): 48679–92. doi: 10.1074/jbc.M106759200 . PMID   11606575.
  85. ↑ Olayioye MA, Graus-Porta D, Beerli RR, Rohrer J, Gay B, Hynes NE (September 1998). "ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner". Molecular and Cellular Biology. 18 (9): 5042–51. doi:10.1128/mcb.18.9.5042. PMC   109089 . PMID   9710588.
  86. ↑ Romero F, Ramos-Morales F, Domínguez A, Rios RM, Schweighoffer F, Tocqué B, Pintor-Toro JA, Fischer S, Tortolero M (March 1998). "Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA". The Journal of Biological Chemistry. 273 (13): 7776–81. doi: 10.1074/jbc.273.13.7776 . PMID   9516488.
  87. ↑ Liu YF, Deth RC, Devys D (March 1997). "SH3 domain-dependent association of huntingtin with epidermal growth factor receptor signaling complexes". The Journal of Biological Chemistry. 272 (13): 8121–4. doi: 10.1074/jbc.272.13.8121 . PMID   9079622.
  88. ↑ Kavanaugh WM, Pot DA, Chin SM, Deuter-Reinhard M, Jefferson AB, Norris FA, Masiarz FR, Cousens LS, Majerus PW, Williams LT (April 1996). "Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2". Current Biology. 6 (4): 438–45. Bibcode:1996CBio....6..438K. doi: 10.1016/s0960-9822(02)00511-0 . PMID   8723348. S2CID   15858192.
  89. 1 2 3 Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E (December 1995). "Involvement of Janus kinases in the insulin signaling pathway". European Journal of Biochemistry. 234 (2): 656–60. doi: 10.1111/j.1432-1033.1995.656_b.x . PMID   8536716.
  90. 1 2 Skolnik EY, Lee CH, Batzer A, Vicentini LM, Zhou M, Daly R, Myers MJ, Backer JM, Ullrich A, White MF (May 1993). "The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling". The EMBO Journal. 12 (5): 1929–36. doi:10.1002/j.1460-2075.1993.tb05842.x. PMC   413414 . PMID   8491186.
  91. ↑ Morrison KB, Tognon CE, Garnett MJ, Deal C, Sorensen PH (August 2002). "ETV6-NTRK3 transformation requires insulin-like growth factor 1 receptor signaling and is associated with constitutive IRS-1 tyrosine phosphorylation". Oncogene. 21 (37): 5684–95. doi:10.1038/sj.onc.1205669. PMID   12173038. S2CID   2899858.
  92. ↑ Bunnell SC, Diehn M, Yaffe MB, Findell PR, Cantley LC, Berg LJ (January 2000). "Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade". The Journal of Biological Chemistry. 275 (3): 2219–30. doi: 10.1074/jbc.275.3.2219 . PMID   10636929.
  93. ↑ Andreotti AH, Bunnell SC, Feng S, Berg LJ, Schreiber SL (January 1997). "Regulatory intramolecular association in a tyrosine kinase of the Tec family". Nature. 385 (6611): 93–7. Bibcode:1997Natur.385...93A. doi:10.1038/385093a0. PMID   8985255. S2CID   25356409.
  94. ↑ Kim H, Lee YH, Won J, Yun Y (September 2001). "Through induction of juxtaposition and tyrosine kinase activity of Jak1, X-gene product of hepatitis B virus stimulates Ras and the transcriptional activation through AP-1, NF-kappaB, and SRE enhancers". Biochemical and Biophysical Research Communications. 286 (5): 886–94. doi:10.1006/bbrc.2001.5496. PMID   11527382.
  95. ↑ Chauhan D, Kharbanda SM, Ogata A, Urashima M, Frank D, Malik N, Kufe DW, Anderson KC (December 1995). "Oncostatin M induces association of Grb2 with Janus kinase JAK2 in multiple myeloma cells". The Journal of Experimental Medicine. 182 (6): 1801–6. doi:10.1084/jem.182.6.1801. PMC   2192257 . PMID   7500025.
  96. ↑ Shen Z, Batzer A, Koehler JA, Polakis P, Schlessinger J, Lydon NB, Moran MF (August 1999). "Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src". Oncogene. 18 (33): 4647–53. doi:10.1038/sj.onc.1203079. PMID   10467411. S2CID   19801963.
  97. ↑ Paz PE, Wang S, Clarke H, Lu X, Stokoe D, Abo A (June 2001). "Mapping the Zap-70 phosphorylation sites on LAT (linker for activation of T cells) required for recruitment and activation of signalling proteins in T cells". The Biochemical Journal. 356 (Pt 2): 461–71. doi:10.1042/0264-6021:3560461. PMC   1221857 . PMID   11368773.
  98. ↑ Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE (January 1998). "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation". Cell. 92 (1): 83–92. doi: 10.1016/S0092-8674(00)80901-0 . PMID   9489702. S2CID   1806525.
  99. ↑ Perez-Villar JJ, Whitney GS, Sitnick MT, Dunn RJ, Venkatesan S, O'Day K, Schieven GL, Lin TA, Kanner SB (August 2002). "Phosphorylation of the linker for activation of T-cells by Itk promotes recruitment of Vav". Biochemistry. 41 (34): 10732–40. doi:10.1021/bi025554o. PMID   12186560.
  100. 1 2 Robinson A, Gibbins J, Rodríguez-Liñares B, Finan PM, Wilson L, Kellie S, Findell P, Watson SP (July 1996). "Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking". Blood. 88 (2): 522–30. doi: 10.1182/blood.V88.2.522.bloodjournal882522 . PMID   8695800.
  101. ↑ Hendricks-Taylor LR, Motto DG, Zhang J, Siraganian RP, Koretzky GA (January 1997). "SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells". The Journal of Biological Chemistry. 272 (2): 1363–7. doi: 10.1074/jbc.272.2.1363 . PMID   8995445.
  102. ↑ Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K (May 1999). "Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT". The Journal of Experimental Medicine. 189 (9): 1383–90. doi:10.1084/jem.189.9.1383. PMC   2193052 . PMID   10224278.
  103. ↑ Lim RW, Halpain S (July 2000). "Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein". The Journal of Biological Chemistry. 275 (27): 20578–87. doi: 10.1074/jbc.M001887200 . PMID   10781592.
  104. ↑ Zamora-Leon SP, Lee G, Davies P, Shafit-Zagardo B (October 2001). "Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2". The Journal of Biological Chemistry. 276 (43): 39950–8. doi: 10.1074/jbc.M107807200 . PMID   11546790.
  105. ↑ Pomérance M, Multon MC, Parker F, Venot C, Blondeau JP, Tocqué B, Schweighoffer F (September 1998). "Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor". The Journal of Biological Chemistry. 273 (38): 24301–4. doi: 10.1074/jbc.273.38.24301 . PMID   9733714.
  106. ↑ Oehrl W, Kardinal C, Ruf S, Adermann K, Groffen J, Feng GS, Blenis J, Tan TH, Feller SM (October 1998). "The germinal center kinase (GCK)-related protein kinases HPK1 and KHS are candidates for highly selective signal transducers of Crk family adapter proteins". Oncogene. 17 (15): 1893–901. doi:10.1038/sj.onc.1202108. PMID   9788432. S2CID   19885101.
  107. ↑ Anafi M, Kiefer F, Gish GD, Mbamalu G, Iscove NN, Pawson T (October 1997). "SH2/SH3 adaptor proteins can link tyrosine kinases to a Ste20-related protein kinase, HPK1". The Journal of Biological Chemistry. 272 (44): 27804–11. doi: 10.1074/jbc.272.44.27804 . PMID   9346925.
  108. ↑ Ling P, Yao Z, Meyer CF, Wang XS, Oehrl W, Feller SM, Tan TH (February 1999). "Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase". Molecular and Cellular Biology. 19 (2): 1359–68. doi:10.1128/mcb.19.2.1359. PMC   116064 . PMID   9891069.
  109. ↑ Ling P, Meyer CF, Redmond LP, Shui JW, Davis B, Rich RR, Hu MC, Wange RL, Tan TH (June 2001). "Involvement of hematopoietic progenitor kinase 1 in T cell receptor signaling". The Journal of Biological Chemistry. 276 (22): 18908–14. doi: 10.1074/jbc.M101485200 . PMID   11279207.
  110. ↑ Wiederhold T, Lee MF, James M, Neujahr R, Smith N, Murthy A, Hartwig J, Gusella JF, Ramesh V (November 2004). "Magicin, a novel cytoskeletal protein associates with the NF2 tumor suppressor merlin and Grb2". Oncogene. 23 (54): 8815–25. doi: 10.1038/sj.onc.1208110 . PMID   15467741.
  111. ↑ Li BQ, Wang MH, Kung HF, Ronsin C, Breathnach R, Leonard EJ, Kamata T (November 1995). "Macrophage-stimulating protein activates Ras by both activation and translocation of SOS nucleotide exchange factor". Biochemical and Biophysical Research Communications. 216 (1): 110–8. doi:10.1006/bbrc.1995.2598. PMID   7488076.
  112. ↑ Iwama A, Yamaguchi N, Suda T (November 1996). "STK/RON receptor tyrosine kinase mediates both apoptotic and growth signals via the multifunctional docking site conserved among the HGF receptor family". The EMBO Journal. 15 (21): 5866–75. doi:10.1002/j.1460-2075.1996.tb00973.x. PMC   452340 . PMID   8918464.
  113. 1 2 Pandey P, Kharbanda S, Kufe D (September 1995). "Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein". Cancer Research. 55 (18): 4000–3. PMID   7664271.
  114. ↑ Saleem A, Datta R, Yuan ZM, Kharbanda S, Kufe D (December 1995). "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth & Differentiation. 6 (12): 1651–8. PMID   9019171.
  115. ↑ Kharbanda S, Saleem A, Shafman T, Emoto Y, Taneja N, Rubin E, Weichselbaum R, Woodgett J, Avruch J, Kyriakis J (August 1995). "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". The Journal of Biological Chemistry. 270 (32): 18871–4. doi: 10.1074/jbc.270.32.18871 . PMID   7642542.
  116. ↑ Satoh S, Tominaga T (October 2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". The Journal of Biological Chemistry. 276 (42): 39290–4. doi: 10.1074/jbc.M107026200 . PMID   11509578.
  117. ↑ Fukuoka M, Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T (February 2001). "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42". The Journal of Cell Biology. 152 (3): 471–82. doi:10.1083/jcb.152.3.471. PMC   2196001 . PMID   11157975.
  118. ↑ Sasaki A, Hata K, Suzuki S, Sawada M, Wada T, Yamaguchi K, Obinata M, Tateno H, Suzuki H, Miyagi T (July 2003). "Overexpression of plasma membrane-associated sialidase attenuates insulin signaling in transgenic mice". The Journal of Biological Chemistry. 278 (30): 27896–902. doi: 10.1074/jbc.M212200200 . PMID   12730204.
  119. ↑ Arvidsson AK, Rupp E, Nånberg E, Downward J, Rönnstrand L, Wennström S, Schlessinger J, Heldin CH, Claesson-Welsh L (October 1994). "Tyr-716 in the platelet-derived growth factor beta-receptor kinase insert is involved in GRB2 binding and Ras activation". Molecular and Cellular Biology. 14 (10): 6715–26. doi:10.1128/mcb.14.10.6715. PMC   359202 . PMID   7935391.
  120. 1 2 Tang J, Feng GS, Li W (October 1997). "Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor". Oncogene. 15 (15): 1823–32. doi: 10.1038/sj.onc.1201351 . PMID   9362449.
  121. ↑ Saleem A, Kharbanda S, Yuan ZM, Kufe D (May 1995). "Monocyte colony-stimulating factor stimulates binding of phosphatidylinositol 3-kinase to Grb2.Sos complexes in human monocytes". The Journal of Biological Chemistry. 270 (18): 10380–3. doi: 10.1074/jbc.270.18.10380 . PMID   7737969.
  122. ↑ Wang J, Auger KR, Jarvis L, Shi Y, Roberts TM (May 1995). "Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase". The Journal of Biological Chemistry. 270 (21): 12774–80. doi: 10.1074/jbc.270.21.12774 . PMID   7759531.
  123. ↑ Pei Z, Maloney JA, Yang L, Williamson JR (September 1997). "A new function for phospholipase C-gamma1: coupling to the adaptor protein GRB2". Archives of Biochemistry and Biophysics. 345 (1): 103–10. doi: 10.1006/abbi.1997.0245 . PMID   9281317.
  124. 1 2 Nel AE, Gupta S, Lee L, Ledbetter JA, Kanner SB (August 1995). "Ligation of the T-cell antigen receptor (TCR) induces association of hSos1, ZAP-70, phospholipase C-gamma 1, and other phosphoproteins with Grb2 and the zeta-chain of the TCR". The Journal of Biological Chemistry. 270 (31): 18428–36. doi: 10.1074/jbc.270.31.18428 . PMID   7629168.
  125. ↑ Scholler JK, Perez-Villar JJ, O'Day K, Kanner SB (August 2000). "Engagement of the T lymphocyte antigen receptor regulates association of son-of-sevenless homologues with the SH3 domain of phospholipase Cgamma1". European Journal of Immunology. 30 (8): 2378–87. doi: 10.1002/1521-4141(2000)30:8<2378::AID-IMMU2378>3.0.CO;2-E . PMID   10940929.
  126. ↑ Sieg DJ, Hauck CR, Ilic D, Klingbeil CK, Schaefer E, Damsky CH, Schlaepfer DD (May 2000). "FAK integrates growth-factor and integrin signals to promote cell migration". Nature Cell Biology. 2 (5): 249–56. doi:10.1038/35010517. PMID   10806474. S2CID   7102625.
  127. ↑ Hildebrand JD, Taylor JM, Parsons JT (June 1996). "An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase". Molecular and Cellular Biology. 16 (6): 3169–78. doi:10.1128/mcb.16.6.3169. PMC   231310 . PMID   8649427.
  128. ↑ Messina S, Onofri F, Bongiorno-Borbone L, Giovedì S, Valtorta F, Girault JA, Benfenati F (January 2003). "Specific interactions of neuronal focal adhesion kinase isoforms with Src kinases and amphiphysin". Journal of Neurochemistry. 84 (2): 253–65. doi: 10.1046/j.1471-4159.2003.01519.x . PMID   12558988.
  129. ↑ Arold ST, Hoellerer MK, Noble ME (March 2002). "The structural basis of localization and signaling by the focal adhesion targeting domain". Structure. 10 (3): 319–27. doi: 10.1016/s0969-2126(02)00717-7 . PMID   12005431.
  130. 1 2 Zhang S, Mantel C, Broxmeyer HE (March 1999). "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells". Journal of Leukocyte Biology. 65 (3): 372–80. doi: 10.1002/jlb.65.3.372 . PMID   10080542. S2CID   38211235.
  131. 1 2 3 Ganju RK, Brubaker SA, Chernock RD, Avraham S, Groopman JE (June 2000). "Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk". The Journal of Biological Chemistry. 275 (23): 17263–8. doi: 10.1074/jbc.M000689200 . PMID   10747947.
  132. ↑ Bennett AM, Tang TL, Sugimoto S, Walsh CT, Neel BG (July 1994). "Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras". Proceedings of the National Academy of Sciences of the United States of America. 91 (15): 7335–9. Bibcode:1994PNAS...91.7335B. doi: 10.1073/pnas.91.15.7335 . PMC   44394 . PMID   8041791.
  133. ↑ Yin T, Shen R, Feng GS, Yang YC (January 1997). "Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases". The Journal of Biological Chemistry. 272 (2): 1032–7. doi: 10.1074/jbc.272.2.1032 . PMID   8995399.
  134. ↑ Tang H, Zhao ZJ, Huang XY, Landon EJ, Inagami T (April 1999). "Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells". The Journal of Biological Chemistry. 274 (18): 12401–7. doi: 10.1074/jbc.274.18.12401 . PMID   10212213.
  135. ↑ Hadari YR, Kouhara H, Lax I, Schlessinger J (July 1998). "Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation". Molecular and Cellular Biology. 18 (7): 3966–73. doi:10.1128/mcb.18.7.3966. PMC   108981 . PMID   9632781.
  136. ↑ Wong L, Johnson GR (August 1996). "Epidermal growth factor induces coupling of protein-tyrosine phosphatase 1D to GRB2 via the COOH-terminal SH3 domain of GRB2". The Journal of Biological Chemistry. 271 (35): 20981–4. doi: 10.1074/jbc.271.35.20981 . PMID   8702859.
  137. ↑ Charest A, Wagner J, Kwan M, Tremblay ML (April 1997). "Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2". Oncogene. 14 (14): 1643–51. doi:10.1038/sj.onc.1201008. PMID   9135065. S2CID   438581.
  138. ↑ Goldstein BJ, Bittner-Kowalczyk A, White MF, Harbeck M (February 2000). "Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein". The Journal of Biological Chemistry. 275 (6): 4283–9. doi: 10.1074/jbc.275.6.4283 . PMID   10660596.
  139. ↑ Liu F, Hill DE, Chernoff J (December 1996). "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)". The Journal of Biological Chemistry. 271 (49): 31290–5. doi: 10.1074/jbc.271.49.31290 . PMID   8940134.
  140. ↑ Kon-Kozlowski M, Pani G, Pawson T, Siminovitch KA (February 1996). "The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells". The Journal of Biological Chemistry. 271 (7): 3856–62. doi: 10.1074/jbc.271.7.3856 . PMID   8632004.
  141. ↑ den Hertog J, Hunter T (June 1996). "Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains". The EMBO Journal. 15 (12): 3016–27. doi:10.1002/j.1460-2075.1996.tb00665.x. PMC   450243 . PMID   8670803.
  142. ↑ den Hertog J, Tracy S, Hunter T (July 1994). "Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo". The EMBO Journal. 13 (13): 3020–32. doi:10.1002/j.1460-2075.1994.tb06601.x. PMC   395191 . PMID   7518772.
  143. ↑ Zheng XM, Resnick RJ, Shalloway D (June 2002). "Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation". The Journal of Biological Chemistry. 277 (24): 21922–9. doi: 10.1074/jbc.M201394200 . PMC   5641391 . PMID   11923305.
  144. ↑ Smit L, van der Horst G, Borst J (April 1996). "Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors". The Journal of Biological Chemistry. 271 (15): 8564–9. doi: 10.1074/jbc.271.15.8564 . PMID   8621483.
  145. ↑ Tanaka S, Morishita T, Hashimoto Y, Hattori S, Nakamura S, Shibuya M, Matuoka K, Takenawa T, Kurata T, Nagashima K (April 1994). "C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins". Proceedings of the National Academy of Sciences of the United States of America. 91 (8): 3443–7. Bibcode:1994PNAS...91.3443T. doi: 10.1073/pnas.91.8.3443 . PMC   43593 . PMID   7512734.
  146. ↑ Borrello MG, Pelicci G, Arighi E, De Filippis L, Greco A, Bongarzone I, Rizzetti M, Pelicci PG, Pierotti MA (June 1994). "The oncogenic versions of the Ret and Trk tyrosine kinases bind Shc and Grb2 adaptor proteins". Oncogene. 9 (6): 1661–8. PMID   8183561.
  147. ↑ Pandey A, Duan H, Di Fiore PP, Dixit VM (September 1995). "The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10". The Journal of Biological Chemistry. 270 (37): 21461–3. doi: 10.1074/jbc.270.37.21461 . PMID   7665556.
  148. ↑ Qian X, Riccio A, Zhang Y, Ginty DD (November 1998). "Identification and characterization of novel substrates of Trk receptors in developing neurons". Neuron. 21 (5): 1017–29. doi: 10.1016/s0896-6273(00)80620-0 . PMID   9856458. S2CID   12354383.
  149. ↑ Kotani K, Wilden P, Pillay TS (October 1998). "SH2-Balpha is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase". The Biochemical Journal. 335 (1): 103–9. doi:10.1042/bj3350103. PMC   1219757 . PMID   9742218.
  150. ↑ Gout I, Middleton G, Adu J, Ninkina NN, Drobot LB, Filonenko V, Matsuka G, Davies AM, Waterfield M, Buchman VL (August 2000). "Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein". The EMBO Journal. 19 (15): 4015–25. doi:10.1093/emboj/19.15.4015. PMC   306608 . PMID   10921882.
  151. ↑ Borinstein SC, Hyatt MA, Sykes VW, Straub RE, Lipkowitz S, Boulter J, Bogler O (December 2000). "SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins". Cellular Signalling. 12 (11–12): 769–79. doi:10.1016/s0898-6568(00)00129-7. PMID   11152963.
  152. 1 2 Satoh T, Kato J, Nishida K, Kaziro Y (May 1996). "Tyrosine phosphorylation of ACK in response to temperature shift-down, hyperosmotic shock, and epidermal growth factor stimulation". FEBS Letters. 386 (2–3): 230–4. doi: 10.1016/0014-5793(96)00449-8 . PMID   8647288. S2CID   23523548.
  153. ↑ Fixman ED, Fournier TM, Kamikura DM, Naujokas MA, Park M (May 1996). "Pathways downstream of Shc and Grb2 are required for cell transformation by the tpr-Met oncoprotein". The Journal of Biological Chemistry. 271 (22): 13116–22. doi: 10.1074/jbc.271.22.13116 . PMID   8662733.
  154. ↑ Ishihara H, Sasaoka T, Ishiki M, Takata Y, Imamura T, Usui I, Langlois WJ, Sawa T, Kobayashi M (April 1997). "Functional importance of Shc tyrosine 317 on insulin signaling in Rat1 fibroblasts expressing insulin receptors". The Journal of Biological Chemistry. 272 (14): 9581–6. doi: 10.1074/jbc.272.14.9581 . PMID   9083103.
  155. ↑ Fournier E, Blaikie P, Rosnet O, Margolis B, Birnbaum D, Borg JP (January 1999). "Role of tyrosine residues and protein interaction domains of SHC adaptor in VEGF receptor 3 signaling". Oncogene. 18 (2): 507–14. doi: 10.1038/sj.onc.1202315 . PMID   9927207.
  156. ↑ Ravichandran KS, Burakoff SJ (January 1994). "The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation". The Journal of Biological Chemistry. 269 (3): 1599–602. doi: 10.1016/S0021-9258(17)42066-7 . PMID   8294403.
  157. ↑ Lamprecht R, Farb CR, LeDoux JE (November 2002). "Fear memory formation involves p190 RhoGAP and ROCK proteins through a GRB2-mediated complex". Neuron. 36 (4): 727–38. doi: 10.1016/s0896-6273(02)01047-4 . PMID   12441060. S2CID   13199381.
  158. 1 2 Park RK, Izadi KD, Deo YM, Durden DL (September 1999). "Role of Src in the modulation of multiple adaptor proteins in FcalphaRI oxidant signaling". Blood. 94 (6): 2112–20. doi:10.1182/blood.V94.6.2112. PMID   10477741.
  159. ↑ Sakaguchi K, Okabayashi Y, Kasuga M (April 2001). "Shc mediates ligand-induced internalization of epidermal growth factor receptors". Biochemical and Biophysical Research Communications. 282 (5): 1154–60. doi:10.1006/bbrc.2001.4680. PMID   11302736.
  160. ↑ Hallak H, Seiler AE, Green JS, Henderson A, Ross BN, Rubin R (July 2001). "Inhibition of insulin-like growth factor-I signaling by ethanol in neuronal cells". Alcoholism: Clinical and Experimental Research. 25 (7): 1058–64. doi: 10.1111/j.1530-0277.2001.tb02317.x . PMID   11505033.
  161. ↑ Yokote K, Mori S, Hansen K, McGlade J, Pawson T, Heldin CH, Claesson-Welsh L (May 1994). "Direct interaction between Shc and the platelet-derived growth factor beta-receptor". The Journal of Biological Chemistry. 269 (21): 15337–43. doi: 10.1016/S0021-9258(17)36611-5 . PMID   8195171.
  162. ↑ Lazar DF, Knez JJ, Medof ME, Cuatrecasas P, Saltiel AR (October 1994). "Stimulation of glycogen synthesis by insulin in human erythroleukemia cells requires the synthesis of glycosyl-phosphatidylinositol". Proceedings of the National Academy of Sciences of the United States of America. 91 (21): 9665–9. Bibcode:1994PNAS...91.9665L. doi: 10.1073/pnas.91.21.9665 . PMC   44877 . PMID   7524086.
  163. ↑ VanderKuur J, Allevato G, Billestrup N, Norstedt G, Carter-Su C (March 1995). "Growth hormone-promoted tyrosyl phosphorylation of SHC proteins and SHC association with Grb2". The Journal of Biological Chemistry. 270 (13): 7587–93. doi: 10.1074/jbc.270.13.7587 . PMID   7535773.
  164. ↑ Kanai M, Göke M, Tsunekawa S, Podolsky DK (March 1997). "Signal transduction pathway of human fibroblast growth factor receptor 3. Identification of a novel 66-kDa phosphoprotein". The Journal of Biological Chemistry. 272 (10): 6621–8. doi: 10.1074/jbc.272.10.6621 . PMID   9045692.
  165. 1 2 Spivak-Kroizman T, Mohammadi M, Hu P, Jaye M, Schlessinger J, Lax I (May 1994). "Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells". The Journal of Biological Chemistry. 269 (20): 14419–23. doi: 10.1016/S0021-9258(17)36639-5 . PMID   7514169.
  166. ↑ Giordano V, De Falco G, Chiari R, Quinto I, Pelicci PG, Bartholomew L, Delmastro P, Gadina M, Scala G (May 1997). "Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase". Journal of Immunology. 158 (9): 4097–103. doi: 10.4049/jimmunol.158.9.4097 . PMID   9126968. S2CID   44339682.
  167. 1 2 Germani A, Romero F, Houlard M, Camonis J, Gisselbrecht S, Fischer S, Varin-Blank N (May 1999). "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways". Molecular and Cellular Biology. 19 (5): 3798–807. doi:10.1128/mcb.19.5.3798. PMC   84217 . PMID   10207103.
  168. ↑ Li N, Batzer A, Daly R, Yajnik V, Skolnik E, Chardin P, Bar-Sagi D, Margolis B, Schlessinger J (May 1993). "Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling". Nature. 363 (6424): 85–8. Bibcode:1993Natur.363...85L. doi:10.1038/363085a0. PMID   8479541. S2CID   4323174.
  169. ↑ Reif K, Buday L, Downward J, Cantrell DA (May 1994). "SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases". The Journal of Biological Chemistry. 269 (19): 14081–7. doi: 10.1016/S0021-9258(17)36757-1 . PMID   8188688.
  170. ↑ D'Angelo G, Martini JF, Iiri T, Fantl WJ, Martial J, Weiner RI (May 1999). "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Molecular Endocrinology. 13 (5): 692–704. doi: 10.1210/mend.13.5.0280 . PMID   10319320.
  171. ↑ Tong XK, Hussain NK, de Heuvel E, Kurakin A, Abi-Jaoude E, Quinn CC, Olson MF, Marais R, Baranes D, Kay BK, McPherson PS (March 2000). "The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain". The EMBO Journal. 19 (6): 1263–71. doi:10.1093/emboj/19.6.1263. PMC   305667 . PMID   10716926.
  172. ↑ Chin H, Saito T, Arai A, Yamamoto K, Kamiyama R, Miyasaka N, Miura O (October 1997). "Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells". Biochemical and Biophysical Research Communications. 239 (2): 412–7. doi:10.1006/bbrc.1997.7480. PMID   9344843.
  173. ↑ Wan KF, Sambi BS, Tate R, Waters C, Pyne NJ (May 2003). "The inhibitory gamma subunit of the type 6 retinal cGMP phosphodiesterase functions to link c-Src and G-protein-coupled receptor kinase 2 in a signaling unit that regulates p42/p44 mitogen-activated protein kinase by epidermal growth factor". The Journal of Biological Chemistry. 278 (20): 18658–63. doi: 10.1074/jbc.M212103200 . PMID   12624098.
  174. ↑ Kato-Stankiewicz J, Ueda S, Kataoka T, Kaziro Y, Satoh T (June 2001). "Epidermal growth factor stimulation of the ACK1/Dbl pathway in a Cdc42 and Grb2-dependent manner". Biochemical and Biophysical Research Communications. 284 (2): 470–7. doi:10.1006/bbrc.2001.5004. PMID   11394904.
  175. ↑ Song C, Perides G, Liu YF (February 2002). "Expression of full-length polyglutamine-expanded Huntingtin disrupts growth factor receptor signaling in rat pheochromocytoma (PC12) cells". The Journal of Biological Chemistry. 277 (8): 6703–7. doi: 10.1074/jbc.M110338200 . PMID   11733534.
  176. ↑ MacDonald JI, Gryz EA, Kubu CJ, Verdi JM, Meakin SO (June 2000). "Direct binding of the signaling adapter protein Grb2 to the activation loop tyrosines on the nerve growth factor receptor tyrosine kinase, TrkA". The Journal of Biological Chemistry. 275 (24): 18225–33. doi: 10.1074/jbc.M001862200 . PMID   10748052.
  177. ↑ Song JS, Gomez J, Stancato LF, Rivera J (October 1996). "Association of a p95 Vav-containing signaling complex with the FcepsilonRI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex". The Journal of Biological Chemistry. 271 (43): 26962–70. doi: 10.1074/jbc.271.43.26962 . PMID   8900182.
  178. ↑ Ye ZS, Baltimore D (December 1994). "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proceedings of the National Academy of Sciences of the United States of America. 91 (26): 12629–33. Bibcode:1994PNAS...9112629Y. doi: 10.1073/pnas.91.26.12629 . PMC   45492 . PMID   7809090.
  179. ↑ Zeng L, Sachdev P, Yan L, Chan JL, Trenkle T, McClelland M, Welsh J, Wang LH (December 2000). "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation". Molecular and Cellular Biology. 20 (24): 9212–24. doi:10.1128/mcb.20.24.9212-9224.2000. PMC   102179 . PMID   11094073.
  180. ↑ Banin S, Truong O, Katz DR, Waterfield MD, Brickell PM, Gout I (August 1996). "Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases". Current Biology. 6 (8): 981–8. Bibcode:1996CBio....6..981B. doi: 10.1016/s0960-9822(02)00642-5 . PMID   8805332. S2CID   162267.
  181. ↑ She HY, Rockow S, Tang J, Nishimura R, Skolnik EY, Chen M, Margolis B, Li W (September 1997). "Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells". Molecular Biology of the Cell. 8 (9): 1709–21. doi:10.1091/mbc.8.9.1709. PMC   305731 . PMID   9307968.

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