E6-AP/UBE3A protein acts as a ubiquitin ligase toward SOX9 protein

Takako Hattori, Tetsuya Kishino, Shelley Stephen, Heidi Eberspaecher, Sayumi Maki, Masaharu Takigawa, Benoit De Crombrugghe, Hideyo Yasuda

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Background: Although the ubiquitin-proteasome pathway is thought to regulate the level of SOX9, the ubiquitin ligase involved has not yet been determined. Results: E6-AP/UBE3A was found to bind and ubiquitinate SOX9. Conclusion: E6-AP/UBE3A functions as a ubiquitin ligase toward SOX9 both in vitro and in vivo. Significance: These data provide the regulatory mechanism of the SOX9 level in chondrocytes by ubiquitin ligase.

Original languageEnglish
Pages (from-to)35138-35148
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number49
DOIs
Publication statusPublished - Dec 6 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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  • Cite this

    Hattori, T., Kishino, T., Stephen, S., Eberspaecher, H., Maki, S., Takigawa, M., De Crombrugghe, B., & Yasuda, H. (2013). E6-AP/UBE3A protein acts as a ubiquitin ligase toward SOX9 protein. Journal of Biological Chemistry, 288(49), 35138-35148. https://doi.org/10.1074/jbc.M113.486795