Ubp8 and SAGA regulate Snf1 AMP kinase activity

Marenda A. Wilson, Evangelia Koutelou, Calley Hirsch, Kadir Akdemir, Andria Schibler, Michelle Craig Barton, Sharon Y.R. Dent

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Posttranslational modifications of histone proteins play important roles in the modulation of gene expression. The Saccharomyces cerevisiae (yeast) 2-MDa SAGA (Spt-Ada-Gcn5) complex, a well-studied multisubunit histone modifier, regulates gene expression through Gcn5-mediated histone acetylation and Ubp8-mediated histone deubiquitination. Using a proteomics approach, we determined that the SAGA complex also deubiquitinates nonhistone proteins, including Snf1, an AMP-activated kinase. Ubp8-mediated deubiquitination of Snf1 affects the stability and phosphorylation state of Snf1, thereby affecting Snf1 kinase activity. Others have reported that Gal83 is phosphorylated by Snf1, and we found that deletion of UBP8 causes decreased phosphorylation of Gal83, which is consistent with the effects of Ubp8 loss on Snf1 kinase functions. Overall, our data indicate that SAGA modulates the posttranslational modifications of Snf1 in order to fine-tune gene expression levels.

Original languageEnglish (US)
Pages (from-to)3126-3135
Number of pages10
JournalMolecular and cellular biology
Volume31
Issue number15
DOIs
StatePublished - Aug 2011
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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