[HTML][HTML] A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
Cell, 1998•cell.com
Caveolin-1 functions as a membrane adaptor to link the integrin α 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.
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.
Abstract
Caveolin-1 functions as a membrane adaptor to link the integrin α 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.
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