Protein kinase C‐δ phosphorylates Ebp1 and prevents its proteolytic degradation, enhancing cell survival

作者: Zhixue Liu , Xia Liu , Keiichi I. Nakayama , Keiko Nakayama , Keqiang Ye

DOI: 10.1111/J.1471-4159.2006.04313.X

关键词:

摘要: ErbB3-binding protein (Ebp1) promotes cell survival by preventing apoptotic DNA fragmentation through a complex with active nuclear Akt. Ebp1 phosphorylation kinase C (PKC)-δ mediates its binding to In this study, we show that itself acts as substrate of caspase 3 during the programmed death. PKC-δ on protects it from degradation initiated in cell-free solution. Moreover, is evidently cleaved PKC-δ-deficient cells but not wild-type cells. translated first ATG resistant cleavage; contrast, second and third demonstrates robust degradation, PKC S360 suppresses cleavage 3. can be digested at both D53 D196 sites, appears prerequisite for further site. Compared Ebp1, D196A mutant markedly apoptosis. Thus, antagonizes apoptosis phosphorylating degradation.

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