GSK3β N-terminus binding to p53 promotes its acetylation

Tae Yeon Eom, Richard S. Jope

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The prevalence in human cancers of mutations in p53 exemplifies its crucial role as a tumor suppressor transcription factor. Previous studies have shown that the constitutively active serine/threonine kinase glycogen synthase kinase-3β (GSK3β) associates with the C-terminal basic domain of p53 and regulates its actions. In this study we identified the GSK3β N-terminal amino acids 78-92 as necessary for its association with p53. Inhibitors of GSK3 impaired the acetylation of p53 at Lys373 and Lys382 near the GSK3β binding region in p53, indicating that GSK3β facilitates p53 acetylation. We also found that acetylation of p53 reduced its association with GSK3β, as well as with GSK3α. These results indicate that the N-terminal region of GSK3β binds p53, this association promotes the acetylation of p53, and subsequently acetylated p53 dissociates from GSK3.

Original languageEnglish (US)
Article number14
JournalMolecular Cancer
StatePublished - Mar 5 2009
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Medicine
  • Oncology
  • Cancer Research


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