TEK tyrosine kinase

Last updated
TEK
Protein TEK PDB 1fvr.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TEK , CD202B, TIE-2, TIE2, VMCM, VMCM1, TEK tyrosine kinase, TEK receptor tyrosine kinase, GLC3E
External IDs OMIM: 600221 MGI: 98664 HomoloGene: 397 GeneCards: TEK
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000459
NM_001290077
NM_001290078
NM_001375475
NM_001375476

NM_001290549
NM_001290551
NM_013690

RefSeq (protein)

NP_000450
NP_001277006
NP_001277007
NP_001362404
NP_001362405

NP_001277478
NP_001277480
NP_038718

Location (UCSC) Chr 9: 27.11 – 27.23 Mb Chr 4: 94.63 – 94.76 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Angiopoietin-1 receptor also known as CD202B (cluster of differentiation 202B) is a protein that in humans is encoded by the TEK gene. [5] [6] Also known as TIE2, it is an angiopoietin receptor.

Function

The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. (TEK is closely related to the TIE receptor tyrosine kinase.) [7]

This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. [8] The ligand for the receptor is angiopoietin-1. [7] TEK has also been suggested as a marker for nucleus pulposus progenitor cells, from the intervertebral disc, which upon activation by Angiopoietin-1 starts to multiply and differentiate. [9] [10]

Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis. [7]

In cancer patients, TEK (Tie2) is expressed in a subpopulation of monocytes that home in on the tumor and are essential for the formation of new blood vessels there. [11]

Interactions

TEK tyrosine kinase has been shown to interact with:

See also

Related Research Articles

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

MuSK is a receptor tyrosine kinase required for the formation and maintenance of the neuromuscular junction. It is activated by a nerve-derived proteoglycan called agrin, which is similarly also required for neuromuscular junction formation.

George D. Yancopoulos is a Greek-American biomedical scientist who is the co-founder, president and chief scientific officer of Regeneron Pharmaceuticals.

<span class="mw-page-title-main">Tropomyosin receptor kinase B</span> Protein and coding gene in humans

Tropomyosin receptor kinase B (TrkB), also known as tyrosine receptor kinase B, or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 is a protein that in humans is encoded by the NTRK2 gene. TrkB is a receptor for brain-derived neurotrophic factor (BDNF). Standard pronunciation is "track bee".

<span class="mw-page-title-main">Receptor tyrosine kinase</span> Class of enzymes

Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 58 encode receptor tyrosine kinase proteins. Receptor tyrosine kinases have been shown not only to be key regulators of normal cellular processes but also to have a critical role in the development and progression of many types of cancer. Mutations in receptor tyrosine kinases lead to activation of a series of signalling cascades which have numerous effects on protein expression. Receptor tyrosine kinases are part of the larger family of protein tyrosine kinases, encompassing the receptor tyrosine kinase proteins which contain a transmembrane domain, as well as the non-receptor tyrosine kinases which do not possess transmembrane domains.

<span class="mw-page-title-main">Neurotrophin-3</span> Protein-coding gene in the species Homo sapiens

Neurotrophin-3 is a protein that in humans is encoded by the NTF3 gene.

<span class="mw-page-title-main">Angiopoietin</span> Protein family

Angiopoietin is part of a family of vascular growth factors that play a role in embryonic and postnatal angiogenesis. Angiopoietin signaling most directly corresponds with angiogenesis, the process by which new arteries and veins form from preexisting blood vessels. Angiogenesis proceeds through sprouting, endothelial cell migration, proliferation, and vessel destabilization and stabilization. They are responsible for assembling and disassembling the endothelial lining of blood vessels. Angiopoietin cytokines are involved with controlling microvascular permeability, vasodilation, and vasoconstriction by signaling smooth muscle cells surrounding vessels. There are now four identified angiopoietins: ANGPT1, ANGPT2, ANGPTL3, ANGPT4.

<span class="mw-page-title-main">KIT (gene)</span> Mammalian protein and protein-coding gene

Proto-oncogene c-KIT is the gene encoding the receptor tyrosine kinase protein known as tyrosine-protein kinase KIT, CD117 or mast/stem cell growth factor receptor (SCFR). Multiple transcript variants encoding different isoforms have been found for this gene. KIT was first described by the German biochemist Axel Ullrich in 1987 as the cellular homolog of the feline sarcoma viral oncogene v-kit.

The angiopoietin receptors are receptors that bind angiopoietin. TIE-1 and TIE-2 comprise the cell-surface receptors that bind and are activated by the angiopoietins,. The angiopoietins are protein growth factors required for the formation of blood vessels (angiogenesis).

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

Angiopoietin 1 is a type of angiopoietin and is encoded by the gene ANGPT1.

<span class="mw-page-title-main">ANGPT2</span> Protein-coding gene in the species Homo sapiens

Angiopoietin-2 is a protein that in humans is encoded by the ANGPT2 gene.

<span class="mw-page-title-main">RAS p21 protein activator 1</span> Protein-coding gene in the species Homo sapiens

RAS p21 protein activator 1 or RasGAP, also known as RASA1, is a 120-kDa cytosolic human protein that provides two principal activities:

<span class="mw-page-title-main">EPH receptor B2</span> Protein-coding gene in the species Homo sapiens

Ephrin type-B receptor 2 is a protein that in humans is encoded by the EPHB2 gene.

<span class="mw-page-title-main">EPH receptor A2</span> Protein-coding gene in humans

EPH receptor A2 is a protein that in humans is encoded by the EPHA2 gene.

<span class="mw-page-title-main">Ephrin A1</span> Protein-coding gene in the species Homo sapiens

Ephrin A1 is a protein that in humans is encoded by the EFNA1 gene.

<span class="mw-page-title-main">EPH receptor B1</span> Protein-coding gene in the species Homo sapiens

Ephrin type-B receptor 1 is a protein that in humans is encoded by the EPHB1 gene.

<span class="mw-page-title-main">DOK2</span> Protein-coding gene in the species Homo sapiens

Docking protein 2 is a protein that in humans is encoded by the DOK2 gene.

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

Receptor-type tyrosine-protein phosphatase beta or VE-PTP is an enzyme specifically expressed in endothelial cells that in humans is encoded by the PTPRB gene.

<span class="mw-page-title-main">ANGPT4</span> Protein-coding gene in the species Homo sapiens

Angiopoietin-4 is a protein that in humans is encoded by the ANGPT4 gene.

<span class="mw-page-title-main">FLT4</span> Protein-coding gene in the species Homo sapiens

Fms-related tyrosine kinase 4, also known as FLT4, is a protein which in humans is encoded by the FLT4 gene.

<span class="mw-page-title-main">TIE1</span>

Tyrosine kinase with immunoglobulin-like and EGF-like domains 1 also known as TIE1 is an angiopoietin receptor which in humans is encoded by the TIE1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000120156 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006386 - 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. Partanen J, Armstrong E, Mäkelä TP, Korhonen J, Sandberg M, Renkonen R, Knuutila S, Huebner K, Alitalo K (April 1992). "A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains". Molecular and Cellular Biology. 12 (4): 1698–707. doi:10.1128/mcb.12.4.1698. PMC   369613 . PMID   1312667.
  6. Boon LM, Mulliken JB, Vikkula M, Watkins H, Seidman J, Olsen BR, Warman ML (September 1994). "Assignment of a locus for dominantly inherited venous malformations to chromosome 9p". Human Molecular Genetics. 3 (9): 1583–7. doi:10.1093/hmg/3.9.1583. PMID   7833915.
  7. 1 2 3 "Entrez Gene: TEK TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)".
  8. 1 2 3 Fiedler U, Krissl T, Koidl S, Weiss C, Koblizek T, Deutsch U, et al. (January 2003). "Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the epidermal growth factor-like repeats". The Journal of Biological Chemistry. 278 (3): 1721–7. doi: 10.1074/jbc.M208550200 . PMID   12427764.
  9. Sakai D, Nakamura Y, Nakai T, Mishima T, Kato S, Grad S, et al. (2012). "Exhaustion of nucleus pulposus progenitor cells with ageing and degeneration of the intervertebral disc". Nature Communications. 3: 1264. Bibcode:2012NatCo...3.1264S. doi:10.1038/ncomms2226. PMC   3535337 . PMID   23232394.
  10. Sakai D, Schol J, Bach FC, Tekari A, Sagawa N, Nakamura Y, et al. (June 2018). "Successful fishing for nucleus pulposus progenitor cells of the intervertebral disc across species". JOR Spine. 1 (2): e1018. doi: 10.1002/jsp2.1018 . PMC   6686801 . PMID   31463445.
  11. Venneri MA, De Palma M, Ponzoni M, Pucci F, Scielzo C, Zonari E, et al. (June 2007). "Identification of proangiogenic TIE2-expressing monocytes (TEMs) in human peripheral blood and cancer". Blood. 109 (12): 5276–85. doi: 10.1182/blood-2006-10-053504 . PMID   17327411. S2CID   13999825.
  12. 1 2 Sato A, Iwama A, Takakura N, Nishio H, Yancopoulos GD, Suda T (August 1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". International Immunology. 10 (8): 1217–27. doi: 10.1093/intimm/10.8.1217 . PMID   9723709.
  13. 1 2 Maisonpierre PC, Suri C, Jones PF, Bartunkova S, Wiegand SJ, Radziejewski C, Compton D, McClain J, Aldrich TH, Papadopoulos N, Daly TJ, Davis S, Sato TN, Yancopoulos GD (July 1997). "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis". Science. 277 (5322): 55–60. doi:10.1126/science.277.5322.55. PMID   9204896.
  14. Davis S, Aldrich TH, Jones PF, Acheson A, Compton DL, Jain V, Ryan TE, Bruno J, Radziejewski C, Maisonpierre PC, Yancopoulos GD (December 1996). "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning". Cell. 87 (7): 1161–9. doi: 10.1016/s0092-8674(00)81812-7 . PMID   8980223.
  15. Jones N, Dumont DJ (September 1998). "The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R". Oncogene. 17 (9): 1097–108. doi:10.1038/sj.onc.1202115. PMID   9764820.
  16. Master Z, Jones N, Tran J, Jones J, Kerbel RS, Dumont DJ (November 2001). "Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak". The EMBO Journal. 20 (21): 5919–28. doi:10.1093/emboj/20.21.5919. PMC   125712 . PMID   11689432.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.