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Src‐stimulated IRTKS phosphorylation enhances cell migration
Author(s) -
Chen Gang,
Li Tingting,
Zhang Lantian,
Yi Min,
Chen Fei,
Wang Zhiqin,
Zhang Xin
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.08.005
Subject(s) - proto oncogene tyrosine protein kinase src , phosphorylation , tyrosine phosphorylation , microbiology and biotechnology , sh2 domain , tyrosine kinase , phosphorylation cascade , protein phosphorylation , chemistry , biology , signal transduction , protein kinase a
Insulin receptor tyrosine kinase substrate (IRTKS) has been demonstrated to be a scaffold protein involved in plasma membrane deformation and actin cytoskeleton remodeling. IRTKS is tyrosine phosphorylated in response to insulin stimulation. However, the mechanism and function of IRTKS phosphorylation remains unclear. Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src‐dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src‐stimulated phosphorylation sites on IRTKS. Disruption of Src‐stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src‐stimulated IRTKS phosphorylation is essential for its function in cell motility.