PTPRB

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PTPRB
Protein PTPRB PDB 2ahs.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PTPRB, HPTP-BETA, HPTPB, PTPB, R-PTP-BETA, VEPTP, protein tyrosine phosphatase, receptor type B
External IDs MGI: 97809 HomoloGene: 2125 GeneCards: PTPRB
RNA expression pattern
PBB GE PTPRB 205846 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001109754
NM_001206971
NM_001206972
NM_002837
NM_001330204

NM_029928

RefSeq (protein)

NP_001103224
NP_001193900
NP_001193901
NP_001317133
NP_002828

NP_084204.2
NP_084204

Location (UCSC) Chr 12: 70.52 – 70.64 Mb Chr 10: 116.3 – 116.39 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

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.[3][4]

Function[edit]

VEPTP is a member of the classical protein tyrosine phosphatase (PTP) family. The deletion of the gene in mouse models was shown to be embryonically lethal,[5] thus indicating that it is important for vasculogenesis and blood vessel development. In addition it was shown to participate in adherens junctions and regulate vascular permeability.[6]

Interactions[edit]

VE-PTP contains an extracellular domain composed of multiple fibronectin type_III repeats, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to R3 receptor subtype PTPs. The extracellular region was shown to interact with the angiopoietin receptor Tie-2.[4] and with the adhesion protein VE-cadherin.[7]

VE-PTP was also found to interact with Grb2 and plakoglobin through its cytoplasmatic domain.

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B". 
  4. ^ a b Fachinger G, Deutsch U, Risau W (Oct 1999). "Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2". Oncogene. 18 (43): 5948–5953. doi:10.1038/sj.onc.1202992. PMID 10557082. 
  5. ^ Bäumer S, Keller L, Holtmann A, Funke R, August B, Gamp A, Wolburg H, Wolburg-Buchholz K, Deutsch U, Vestweber D (Jun 2006). "Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development". Blood. 107 (12): 4754–62. doi:10.1182/blood-2006-01-0141. PMID 16514057. 
  6. ^ Broermann A, Winderlich M, Block H, Frye M, Rossaint J, Zarbock A, Cagna G, Linnepe R, Schulte D, Nottebaum AF, Vestweber D (Nov 2011). "Dissociation of VE-PTP from VE-cadherin is required for leukocyte extravasation and for VEGF-induced vascular permeability in vivo". The Journal of Experimental Medicine. 208 (12): 2393–401. doi:10.1084/jem.20110525. PMID 22025303. 
  7. ^ Nawroth R, Poell G, Ranft A, Kloep S, Samulowitz U, Fachinger G, Golding M, Shima DT, Deutsch U, Vestweber D (Sep 2002). "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts". The EMBO Journal. 21 (18): 4885–4895. doi:10.1093/emboj/cdf497. PMC 126293Freely accessible. PMID 12234928. 

Further reading[edit]