Receptor Protein Tyrosine Phosphatase-Receptor Tyrosine Kinase Substrate Screen Identifies EphA2 as a Target for LAR in Cell Migration
作者： H. Lee , A. M. Bennett
DOI: 10.1128/MCB.01708-12
关键词:
摘要: Receptor tyrosine kinases (RTKs) exist in equilibrium between tyrosyl-phosphorylated and dephosphorylated states. Despite a detailed understanding of how RTKs become tyrosyl phosphorylated, much less is known about RTK dephosphorylation. protein phosphatases (RPTPs) can play essential roles the dephosphorylation RTKs. However, complete involvement RPTP subfamily has not been established. In this study, we have employed small interfering RNA (siRNA) screen to identify RPTPs human genome that serve as phosphatases. We observed each induced unique fingerprint phosphorylation among 42 identified EphA2 novel LAR substrate. at phosphotyrosyl 930, uncoupling Nck1 from thereby attenuating EphA2-mediated cell migration. These results demonstrate exerts regulatory suggest complex signaling interplay RPTPs. Furthermore, modulates migration through site-specific
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