The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquitinated and phosphorylated in vivo

Mark G. Goebl, Loretta Goetsch, Breck Byers

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

The transition from G1 to S phase of the cell cycle in Saccharomyces cerevisiae requires the activity of the Ubc3 (Cdc34) ubiquitin-conjugating enzyme. S. cerevisiae cells lacking a functional UBC3 (CDC34) gene are able to execute the Start function that initiates the cell cycle but fail to form a mitotic spindle or enter S phase. The Ubc3 (Cdc34) enzyme has previously been shown to catalyze the attachment of multiple ubiquitin molecules to model substrates, suggesting that the role of this enzyme in cell cycle progression depends on its targeting an endogenous protein(s) for degradation. In this report, we demonstrate that the Ubc3 (Cdc34) protein is itself a substrate for both ubiquitination and phosphorylation. Immunochemical localization of the gene product to the nucleus renders it likely that the relevant substrates similarly reside within the nucleus.

Original languageEnglish (US)
Pages (from-to)3022-3029
Number of pages8
JournalMolecular and cellular biology
Volume14
Issue number5
DOIs
StatePublished - May 1994

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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