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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(More)
ntegrin ␣ 6 ␤ 4 signaling proceeds through Src family kinase (SFK)–mediated phosphorylation of the cytoplasmic tail of ␤ 4, recruitment of Shc, and activation of Ras and phosphoinositide-3 kinase. Upon cessation of signaling, ␣ 6 ␤ 4 mediates assembly of hemidesmosomes. Here, we report that part of ␣ 6 ␤ 4 is incorporated in lipid rafts. Metabolic labeling(More)
e have examined the mechanism and functional significance of hemidesmosome disassembly during normal epithelial cell migration and squamous carcinoma invasion. Our findings indicate that a fraction of EGF receptor (EGF-R) combines with the hemidesmosomal integrin ␣ 6 ␤ 4 in both normal and neoplastic keratinocytes. Activation of the EGF-R causes tyrosine(More)
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