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  5. Molecular Mechanism for Phosphorylated c-MET Recognition of SHIP2 SH2 Domain Revealed by NMR Spectro

Molecular Mechanism for Phosphorylated c-MET Recognition of SHIP2 SH2 Domain Revealed by NMR Spectro

来源 :中国生物化学与分子生物学会第十二届会员代表大会暨2018年全国学术会议 | 被引量 : 0次 | 上传用户：yys68738464
【摘 要】
：
The SH2 domain-containing inositol 5-phosphatase 2(SHIP2)hydrolyzes the 5-phosphate of PtdIns(3,4,5)P3 to produce PtdIns(3,4)P2,playing an essential role in hepatocyte growth factor(HGF)induced cell s
【作 者】
：
Zi Wang Jiang Zhu Yao Nie Rui Hu Maili Liu Yunhuang Yang 
【机 构】
：
State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics,Wuhan Center for Magneti
【出 处】
：
中国生物化学与分子生物学会第十二届会员代表大会暨2018年全国学术会议
【发表日期】
：
2018年10期
【关键词】
：
INPPL1 c-MET SH2 domain NMR structure tyrosine phosphorylation 
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　　The SH2 domain-containing inositol 5-phosphatase 2(SHIP2)hydrolyzes the 5-phosphate of PtdIns(3,4,5)P3 to produce PtdIns(3,4)P2,playing an essential role in hepatocyte growth factor(HGF)induced cell scattering and cell spreading.The role of SHIP2 in cell spreading was suggested to be associated with the binding of SHIP2 with the HGF receptor,c-MET,which is mediated by the SH2 domain of SHIP2 and required the phosphorylation of c-MET at Tyr1356.
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