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Beschreibung

Platelet-derived growth factor receptor beta (EC 2.7.10.1, UniProt P09619, also known as Beta platelet-derived growth factor receptor, Beta-type platelet-derived growth factor receptor, CD140 antigen-like family member B, CD140b, PDGF-R-beta, PDGFR-1, PDGFR-beta, Platelet-derived growth factor receptor 1) is encoded by the PDGFRB (also known as IBGC4, IMF1, PDGFR, PDGFR1) gene (Gene ID 5159) in human. PDGFR-1 is a tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB. PDGF receptors consist of extracellular domains with five immunoglobulin (Ig) - like domains and intracellular parts with kinase domains, which contain characteristic inserts of about 100 amino acid residues without homology to kinases. Ligand binding occurs mainly to Ig-like domains 2 and 3, which causes dimerization of the receptor, which is further stabilized by direct receptor-receptor interactions involving Ig-like domain 4. In the absence of a bound ligand, receptor is present in an inactive conformation. However, upon ligand binding it undergoes dimerization and autophosphorylation on tyrosine residues. PDGFR-1m plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis, and migration. It is also considered to be essential for endothelial cell proliferation, migration and recruitment of pericytes and smooth muscle cells to form blood vessels. PDGFR-1 phosphorylates phospholipase C-gamma 1 (PLCG1), PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of diacylglycerol and IP3 that are involved in calcium mobilization and activation of PKC. Ref.: Heldin C-H (2013). Cell Commun. Signaling 11:97.C1