Article ID Journal Published Year Pages File Type
1939964 Biochemical and Biophysical Research Communications 2006 6 Pages PDF
Abstract

p66Shc protein has been proposed to be an indispensable factor for p53-dependent, mitochondria-mediated apoptosis in mice. Here, we show that p66Shc plays a pro-apoptotic role also in cell lines of human origin such as SaOs-2 and HeLa, where p53 is either absent or inactivated, thus, suggesting that p66Shc pro-apoptotic role is independent from the presence of a functional form of p53. The active form of p66Shc is phosphorylated in Serine 36. We confirm the importance of Serine 36 phosphorylation for p66Shc pro-apoptotic role, and our results suggest that the kinase involved in this process is activated independently from p53.

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