Afadin

Last updated
AFDN
Protein MLLT4 PDB 1t2m.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases AFDN , AF6, MLL-AF6, MLLT4, myeloid/lymphoid or mixed-lineage leukemia; translocated to, 4, afadin, adherens junction formation factor, l-afadin
External IDs OMIM: 159559 MGI: 1314653 HomoloGene: 21202 GeneCards: AFDN
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_010806

RefSeq (protein)

NP_034936

Location (UCSC) Chr 6: 167.83 – 167.97 Mb Chr 17: 13.98 – 14.13 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Afadin is a protein that in humans is encoded by the AFDN gene. [5]

Function

Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998).[supplied by OMIM] [6]

Interactions

Afadin has been shown to interact with:

Related Research Articles

<span class="mw-page-title-main">Vinculin</span> Mammalian protein found in Homo sapiens

In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane.

<span class="mw-page-title-main">DLG1</span> Protein-coding gene in the species Homo sapiens

Discs large homolog 1 (DLG1), also known as synapse-associated protein 97 or SAP97, is a scaffold protein that in humans is encoded by the SAP97 gene.

<span class="mw-page-title-main">Tight junction protein 1</span> Protein found in humans

Zonula occludens-1 ZO-1, also known as Tight junction protein-1 is a 220-kD peripheral membrane protein that is encoded by the TJP1 gene in humans. It belongs to the family of zonula occludens proteins, which are tight junction-associated proteins and of which, ZO-1 is the first to be cloned. It was first isolated in 1986 by Stevenson and Goodenough using a monoclonal antibody raised in rodent liver to recognise a 225-kD polypeptide in whole liver homogenates and in tight junction-enriched membrane fractions. It has a role as a scaffold protein which cross-links and anchors Tight Junction (TJ) strand proteins, which are fibril-like structures within the lipid bilayer, to the actin cytoskeleton.

<span class="mw-page-title-main">Syntenin-1</span> Protein found in humans

Syntenin-1 is a protein that in humans is encoded by the SDCBP gene.

<span class="mw-page-title-main">Poliovirus receptor-related 2</span> Protein-coding gene in the species Homo sapiens

Poliovirus receptor-related 2 (PVRL2), also known as nectin-2 and CD112, is a human plasma membrane glycoprotein.

<span class="mw-page-title-main">Alpha-actinin-4</span> Protein-coding gene in the species Homo sapiens

Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.

<span class="mw-page-title-main">Poliovirus receptor-related 1</span> Protein-coding gene in the species Homo sapiens

Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM).

<span class="mw-page-title-main">SORBS1</span> Protein-coding gene in the species Homo sapiens

CAP/Ponsin protein, also known as Sorbin and SH3 domain-containing protein 1 is a protein that in humans is encoded by the SORBS1 gene. It is part of a small family of adaptor proteins that regulate cell adhesion, growth factor signaling and cytoskeletal formation. It is mainly expressed in heart, skeletal muscle, liver, adipose tissue, and macrophages; in striated muscle tissue, it is localized to costamere structures.

<span class="mw-page-title-main">EPHB3</span> Protein-coding gene in the species Homo sapiens

Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene.

<span class="mw-page-title-main">DLGAP1</span> Protein-coding gene in the species Homo sapiens

Disks large-associated protein 1 (DAP-1), also known as guanylate kinase-associated protein (GKAP), is a protein that in humans is encoded by the DLGAP1 gene. DAP-1 is known to be highly enriched in synaptosomal preparations of the brain, and present in the post-synaptic density.

<span class="mw-page-title-main">UNC13B</span> Protein-coding gene in the species Homo sapiens

Protein unc-13 homolog B is a protein that in humans is encoded by the UNC13B gene.

<span class="mw-page-title-main">RAB3B</span> Protein-coding gene in the species Homo sapiens

Ras-related protein Rab-3B is a protein that in humans is encoded by the RAB3B gene.

<span class="mw-page-title-main">SSX2IP</span> Protein-coding gene in the species Homo sapiens

Afadin- and alpha-actinin-binding protein is a protein that in humans is encoded by the SSX2IP gene. It has been shown that it functions together with WDR8 in centrosome maturation, ensuring proper spindle length and orientation. The SSX2IP-WDR8 complex additionally promotes ciliary vesicle docking during ciliogenesis.

<span class="mw-page-title-main">ERC2 (gene)</span> Protein-coding gene in the species Homo sapiens

ERC protein 2 is a protein that in humans is encoded by the ERC2 gene.

<span class="mw-page-title-main">Catenin alpha-1</span> Protein-coding gene in the species Homo sapiens

αE-catenin, also known as Catenin alpha-1 is a protein that in humans is encoded by the CTNNA1 gene. αE-catenin is highly expressed in cardiac muscle and localizes to adherens junctions at intercalated disc structures where it functions to mediate the anchorage of actin filaments to the sarcolemma. αE-catenin also plays a role in tumor metastasis and skin cell function.

Nectins and Nectin-like molecules (Necl) are families of cellular adhesion molecules involved in Ca2+-independent cellular adhesion.

<span class="mw-page-title-main">RASSF9</span> Protein-coding gene in the species Homo sapiens

Ras association domain-containing protein 9 (RASSF9), also known as PAM COOH-terminal interactor protein 1 (PCIP1) or peptidylglycine alpha-amidating monooxygenase COOH-terminal interactor (PAMCI) is a protein that in humans is encoded by the RASSF9 gene.

<span class="mw-page-title-main">PLEKHA7</span> Protein-coding gene in the species Homo sapiens

PLEKHA7 is an adherens junction (AJ) protein, involved in the junction's integrity and stability.

<span class="mw-page-title-main">Synaptic stabilization</span> Modifying synaptic strength via cell adhesion molecules

Synaptic stabilization is crucial in the developing and adult nervous systems and is considered a result of the late phase of long-term potentiation (LTP). The mechanism involves strengthening and maintaining active synapses through increased expression of cytoskeletal and extracellular matrix elements and postsynaptic scaffold proteins, while pruning less active ones. For example, cell adhesion molecules (CAMs) play a large role in synaptic maintenance and stabilization. Gerald Edelman discovered CAMs and studied their function during development, which showed CAMs are required for cell migration and the formation of the entire nervous system. In the adult nervous system, CAMs play an integral role in synaptic plasticity relating to learning and memory.

<span class="mw-page-title-main">Nectin-3</span>

Nectin-3, also known as nectin cell adhesion molecule 3, is a protein that in humans is encoded by the NECTIN3 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000130396 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000068036 - 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. Prasad R, Gu Y, Alder H, Nakamura T, Canaani O, Saito H, Huebner K, Gale RP, Nowell PC, Kuriyama K (Dec 1993). "Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation". Cancer Research. 53 (23): 5624–8. PMID   8242616.
  6. "Entrez Gene: MLLT4 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4".
  7. Radziwill G, Erdmann RA, Margelisch U, Moelling K (Jul 2003). "The Bcr kinase downregulates Ras signaling by phosphorylating AF-6 and binding to its PDZ domain". Molecular and Cellular Biology. 23 (13): 4663–72. doi:10.1128/mcb.23.13.4663-4672.2003. PMC   164848 . PMID   12808105.
  8. Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K (Aug 1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proceedings of the National Academy of Sciences of the United States of America. 95 (17): 9779–84. Bibcode:1998PNAS...95.9779H. doi: 10.1073/pnas.95.17.9779 . PMC   21413 . PMID   9707552.
  9. Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi: 10.1074/jbc.M002363200 . PMID   10856295.
  10. 1 2 3 Boettner B, Govek EE, Cross J, Van Aelst L (Aug 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 9064–9. Bibcode:2000PNAS...97.9064B. doi: 10.1073/pnas.97.16.9064 . PMC   16822 . PMID   10922060.
  11. 1 2 Yamamoto T, Harada N, Kawano Y, Taya S, Kaibuchi K (May 1999). "In vivo interaction of AF-6 with activated Ras and ZO-1". Biochemical and Biophysical Research Communications. 259 (1): 103–7. doi:10.1006/bbrc.1999.0731. PMID   10334923.
  12. Bégay-Müller V, Ansieau S, Leutz A (Jun 2002). "The LIM domain protein Lmo2 binds to AF6, a translocation partner of the MLL oncogene". FEBS Letters. 521 (1–3): 36–8. doi:10.1016/s0014-5793(02)02814-4. PMID   12067721. S2CID   29461336.
  13. Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y (May 1999). "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein". The Journal of Cell Biology. 145 (3): 539–49. doi:10.1083/jcb.145.3.539. PMC   2185068 . PMID   10225955.
  14. Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y (Apr 2000). "Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities". The Journal of Biological Chemistry. 275 (14): 10291–9. doi: 10.1074/jbc.275.14.10291 . PMID   10744716.
  15. Reymond N, Borg JP, Lecocq E, Adelaide J, Campadelli-Fiume G, Dubreuil P, Lopez M (Sep 2000). "Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family that interacts with afadin". Gene. 255 (2): 347–55. doi:10.1016/s0378-1119(00)00316-4. PMID   11024295.
  16. Su L, Hattori M, Moriyama M, Murata N, Harazaki M, Kaibuchi K, Minato N (Apr 2003). "AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1". The Journal of Biological Chemistry. 278 (17): 15232–8. doi: 10.1074/jbc.M211888200 . hdl: 2433/148462 . PMID   12590145.
  17. Mandai K, Nakanishi H, Satoh A, Takahashi K, Satoh K, Nishioka H, Mizoguchi A, Takai Y (Mar 1999). "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions". The Journal of Cell Biology. 144 (5): 1001–17. doi:10.1083/jcb.144.5.1001. PMC   2148189 . PMID   10085297.
  18. Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (Feb 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". The Journal of Biological Chemistry. 278 (6): 4103–11. doi: 10.1074/jbc.M209832200 . PMID   12446711.
  19. Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K (Dec 1999). "The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin". Genes to Cells. 4 (12): 757–67. doi: 10.1046/j.1365-2443.1999.00297.x . PMID   10620020. S2CID   85747886.
  20. Taya S, Yamamoto T, Kano K, Kawano Y, Iwamatsu A, Tsuchiya T, Tanaka K, Kanai-Azuma M, Wood SA, Mattick JS, Kaibuchi K (Aug 1998). "The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme". The Journal of Cell Biology. 142 (4): 1053–62. doi:10.1083/jcb.142.4.1053. PMC   2132865 . PMID   9722616.

Further reading