Regulation of chemotaxis by the platelet-derived growth factor receptor-β
作者： Vikas Kundra , Jaime A. Escobedo , Andrius Kazlauskas , Ha Kun Kim , Sue Goo Rhee
DOI: 10.1038/367474A0
关键词:
摘要: Chemotaxis is an important component of wound healing, development, immunity and metastasis, yet the signalling pathways that mediate chemotaxis are poorly understood. Platelet-derived growth factor (PDGF) acts both as a mitogen chemoattractant. Upon stimulation, tyrosine kinase PDGF receptor-beta (PDGFR-beta) autophosphorylates forms complex includes SII2(Src homology 2)-domain-containing proteins such phosphatidylinositol-specific phospholipase C-gamma, Ras-GTPase-activating protein (GAP), phosphatidylinositol-3-OH kinase. Specific tyrosine-to-phenylalanine substitutions in PDGFR-beta can prevent binding one SH2-domain-containing without affecting other receptor-associated proteins. Here we use C-gamma mutants to map specific tyrosines involved positive negative regulation towards PDGF-BB homodimer. Our results indicate delicate balance migration-promoting (phospholipase kinase) migration-suppressing (GAP) activities recruited by drive PDGF-BB.
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