Trihydrophobin 1 phosphorylation by c-Src regulates MAPK/ERK signaling and cell migration |
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Authors: | Wu Weibin Sun Zhichao Wu Jingwen Peng Xiaomin Gan Huacheng Zhang Chunyi Ji Lingling Xie Jianhui Zhu Haiyan Ren Shifang Gu Jianxin Zhang Songwen |
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Institution: | Gene Research Center, Shanghai Medical College, Fudan University, Shanghai, China. |
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Abstract: | c-Src activates Ras-MAPK/ERK signaling pathway and regulates cell migration, while trihydrophobin 1 (TH1) inhibits MAPK/ERK activation and cell migration through interaction with A-Raf and PAK1 and inhibiting their kinase activities. Here we show that c-Src interacts with TH1 by GST-pull down assay, coimmunoprecipitation and confocal microscopy assay. The interaction leads to phosphorylation of TH1 at Tyr-6 in vivo and in vitro. Phosphorylation of TH1 decreases its association with A-Raf and PAK1. Further study reveals that Tyr-6 phosphorylation of TH1 reduces its inhibition on MAPK/ERK signaling, enhances c-Src mediated cell migration. Moreover, induced tyrosine phosphorylation of TH1 has been found by EGF and estrogen treatments. Taken together, our findings demonstrate a novel mechanism for the comprehensive regulation of Ras/Raf/MEK/ERK signaling and cell migration involving tyrosine phosphorylation of TH1 by c-Src. |
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