Phosphatase Subfamily PTPRB
Phosphatase Classification: Fold CC1: Superfamily CC1: Family PTP: Subfamily PTPRB
PTPRC (CD45) is a vertebrate-specific receptor PTP involved in immune signaling.
Evolution
PTPRB subfamily is found across metazoan. It has multiple copies per genomes in bilateral.
Domain Structure
Functions
(summary)
PTPRB (VE-PTP)
PTPRB, a.k.a. vascular endothelial protein tyrosine phosphatase (VE-PTP), is expressed specifically in endothelial cells and regulates the spreading and migration of endothelial cells during angiogenesis [1]. PTPRB binds to vascular E-cadherin (VE-cadherin) through an extracellular domain and reduces the tyrosine phosphorylation of VE-cadherin. But, the reduction of tyrosine phosphorylation seems independently of its enzymatic activity, since catalytically inactive mutant form of PTPRB had the same effect on VE-cadherin phosphorylation [2]. PTPRB associates with endothelial cell (EC)-selective receptor tyrosine kinase Tie2, which maintains vascular integrity [3, 4, 5, 6]. PTPRB regulates vascular endothelial growth factor receptor 2 activity thereby modulating the VEGF-response during angiogenesis [7].
PTPRB is intrinsically active and its inactivation is dependent on its ligand pleiotrophin (PTN) which is a platelet-derived growth factor-inducible, 18-kDa heparin-binding cytokine that signals diverse phenotypes in normal and deregulated cellular growth and differentiation [8]. PTPRB is glycosylated protein (phosphacan).
PTPRB mutations are observed in cancers. Its mutations are recurrent in angiosarcoma [9]. PTPRB mediates glial tumor cell adhesion by binding to tenascin C [10].
PTPRB interacts with neuronal receptors and promotes neurite outgrowth [11].
PTPRQ
References
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