Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA , PDGFB and PDGFC and plays an essential role in the regulation of embryonic development , cell proliferation , survival and chemotaxis. Depending on the context , promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract , and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation , secretion of agonists from platelet granules , and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA , homodimeric PDGFB , heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1 , PLCG1 , and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1 ,4 ,5-trisphosphate , mobilization of cytosolic Ca (2+) and the activation of protein kinase C. Phosphorylates PIK3R1 , the regulatory subunit of phosphatidylinositol 3-kinase , and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1 , STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors , and by rapid internalization of the activated receptor.
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