整合素信号传导及锚定依赖性细胞生长中对小窝蛋白-1和相关激酶Fyn的需求。
A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth.
作者信息
Wary K K, Mariotti A, Zurzolo C, Giancotti F G
机构信息
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
出版信息
Cell. 1998 Sep 4;94(5):625-34. doi: 10.1016/s0092-8674(00)81604-9.
Caveolin-1 functions as a membrane adaptor to link the integrin alpha subunit to the tyrosine kinase Fyn. Upon integrin ligation, Fyn is activated and binds, via its SH3 domain, to Shc. Shc is subsequently phosphorylated at tyrosine 317 and recruits Grb2. This sequence of events is necessary to couple integrins to the Ras-ERK pathway and promote cell cycle progression. These findings reveal an unexpected function of caveolin-1 and Fyn in integrin signaling and anchorage-dependent cell growth.
小窝蛋白-1作为一种膜衔接蛋白，将整合素α亚基与酪氨酸激酶Fyn连接起来。整合素连接后，Fyn被激活，并通过其SH3结构域与Shc结合。随后，Shc在酪氨酸317处被磷酸化，并招募Grb2。这一系列事件对于将整合素与Ras-ERK途径偶联并促进细胞周期进程是必要的。这些发现揭示了小窝蛋白-1和Fyn在整合素信号传导及锚定依赖性细胞生长中的意外功能。
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