Mechanism of degradation of CPEB during Xenopus oocyte maturation.

ABSTRACT: CPEB, a cytoplasmic polyadenylation element-binding protein, plays an important role in translational control of maternal mRNAs in early animal development. During Xenopus oocyte maturation, CPEB undergoes a Cdc2-mediated phosphorylation- and ubiquitin-dependent degradation that is required for proper entry into meiosis II. However, the precise mechanism of CPEB degradation, including the identity of the responsible E3 ubiquitin ligase, is not known. Here, we show that the SCF(beta-TrCP) E3 ubiquitin ligase complex targets CPEB for degradation during Xenopus oocyte maturation. beta-TrCP, the F-box protein of SCF(beta-TrCP), specifically binds to a sequence (190)TSGFSS(195) (termed here the TSG motif) of CPEB, thereby targeting CPEB for degradation. beta-TrCP binding depends on phosphorylat

SUBMITTER: Setoyama D 

PROVIDER: S-EPMC2084286 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature