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TEK tyrosine kinase

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Title: TEK tyrosine kinase  
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TEK tyrosine kinase

TEK tyrosine kinase, endothelial

PDB rendering based on 1fvr.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; CD202B; TIE-2; TIE2; VMCM; VMCM1
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Angiopoietin-1 receptor is a protein that in humans is encoded by the TEK gene.[1][2]

TEK has also recently been designated CD202B (cluster of differentiation 202B). The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. 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. The ligand for the receptor is angiopoietin-1. 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. TEK is closely related to the TIE receptor tyrosine kinase.[3]

Interactions

TEK tyrosine kinase has been shown to interact with DOK2,[4][5] Angiopoietin 1[6][7][8][9] and ANGPT2.[6][8][9]

References

  1. ^ Partanen J, Armstrong E, Makela 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". Mol Cell Biol 12 (4): 1698–707.  
  2. ^ Boon LM, Mulliken JB, Vikkula M, Watkins H, Seidman J, Olsen BR, Warman ML (February 1995). "Assignment of a locus for dominantly inherited venous malformations to chromosome 9p". Hum Mol Genet 3 (9): 1583–7.  
  3. ^ "Entrez Gene: TEK TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)". 
  4. ^ Jones, N; Dumont D J (September 1998). "The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R". Oncogene (ENGLAND) 17 (9): 1097–108.  
  5. ^ Master, Z; Jones N; Tran J; Jones J; Kerbel R S; Dumont D J (November 2001). "Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak". EMBO J. (England) 20 (21): 5919–28.  
  6. ^ a b Fiedler, Ulrike; Krissl Tanja, Koidl Stefanie, Weiss Cornelia, Koblizek Thomas, Deutsch Urban, Martiny-Baron Georg, Marmé Dieter, Augustin Hellmut G (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". J. Biol. Chem. (United States) 278 (3): 1721–7.  
  7. ^ Davis, S; Aldrich T H, Jones P F, Acheson A, Compton D L, Jain V, Ryan T E, Bruno J, Radziejewski C, Maisonpierre P C, Yancopoulos G D (December 1996). "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning". Cell (UNITED STATES) 87 (7): 1161–9.  
  8. ^ a b Sato, A; Iwama A; Takakura N; Nishio H; Yancopoulos G D; Suda T (August 1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". Int. Immunol. (ENGLAND) 10 (8): 1217–27.  
  9. ^ a b Maisonpierre, P C; Suri C, Jones P F, Bartunkova S, Wiegand S J, Radziejewski C, Compton D, McClain J, Aldrich T H, Papadopoulos N, Daly T J, Davis S, Sato T N, Yancopoulos G D (July 1997). "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis".  

External links

  • GeneReviews/NCBI/NIH/UW entry on Multiple Cutaneous and Mucosal Venous Malformations

Further reading

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


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