Phosphorylation of the anaphase-promoting complex/Cdc27 is involved in TGF-β signaling

Liyong Zhang, Takeo Fujita, George Wu, Xiao Xiao, Yong Wan*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Loss of TGF-β-induced growth inhibition is a hallmark of many human tumors. Previous studies implied that activation of the anaphase-promoting complex (APC/cyclosome) is involved in the TGF-β signaling pathway, which facilitates the destruction of SnoN, a transcriptional co-suppressor, which leads in turn to the transactivation of TGF-β-responsive genes for cell cycle arrest. The function of APC was demonstrated in TGF-β signal transduction, but the mechanism by which it is activated in response to TGF-β signaling remains unclear. We report here that phosphorylation of Cdc27, a core subunit of APC, in response to TGF-β signaling can facilitate the activation of APC. Wehave demonstrated that casein kinase II (CKII) is involved in the phosphorylation of Cdc27 in response to TGF-β signaling. Depletion of CKII by shRNA abolishes the TGF-β-induced phosphorylation of Cdc27 and subsequent degradation of SnoN. Disruptive mutation of Cdc27 (S154A) attenuates TGF-β-induced SnoN degradation. In addition, expression of a phosphorylation-resistant Cdc27 mutant significantly attenuates TGF-β-induced growth inhibition. Together, the results suggest that phosphorylation of Cdc27 by CKII is involved in TGF-β-induced activation of APC.

Original languageEnglish (US)
Pages (from-to)10041-10050
Number of pages10
JournalJournal of Biological Chemistry
Issue number12
StatePublished - Mar 25 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Cell Biology


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