FAK autophosphorylation

The molecular interactions between PTEN and FAK were studied in glioblastoma and breast cancer cells lacking PTEN. The PTEN trapping mutant bound wild-type FAK, requiring FAK autophosphorylation site Tyr397. In PTEN-mutated cancer cells, FAK phosphorylation was retained even in suspension after detachment from extracellular matrix, accompanied by enhanced PI3-K association with FAK and sustained PI3-K activity. PTEN-mutated cells were resistant to apoptosis in suspension, but most of the cells entered apoptosis after expression of exogenous PTEN or... 

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