Learn More
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)
  • L Girardello, A Mariotti, G Tartaglino-Mazzucchelli
  • 2006
We investigate the Dijkgraaf-Vafa proposal when supersymmetry is broken. We consider U(N) SYM with chiral adjoint matter where the coupling constants in the tree-level su-perpotential are promoted to chiral spurions. The holomorphic part of the low-energy glueball superpotential can still be analyzed. We compute the holomorphic supersymme-try breaking(More)
We 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 alpha6beta4 in both normal and neoplastic keratinocytes. Activation of the EGF-R causes(More)
  • 1