Ubiquitination of the G1 cyclin Cln2p by a Cdc34p-dependent pathway

Raymond J. Deshaies, Vincent Chau, Marc Kirschner

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186 Scopus citations

Abstract

Recombinant G1 cyclin Cln2p can bind to and stimulate the protein kinase activity of p34(CDC28) (Cdc28p) in an extract derived from cyclin-depleted and G1-arrested Saccharomyces cerevisiae cells. Upon activating Cdc28p, Cln2p is extensively phosphorylated and conjugated with multiubiquitin chains. Ubiquitination of Cln2p in vitro requires the Cdc34p ubiquitin-conjugating enzyme, Cdc28p, protein phosphorylation and unidentified factors in yeast extract. Ubiquitination of Cln2p by Cdc34p contributes to the instability of Cln2p in vivo, as the rate of Cln2p degradation is reduced in cdc34(ts) cells. These results provide a molecular framework for G1 cyclin instability and suggest that a multicomponent, regulated pathway specifies the selective ubiquitination of G1 cyclins.

Original languageEnglish (US)
Pages (from-to)303-312
Number of pages10
JournalEMBO Journal
Volume14
Issue number2
DOIs
StatePublished - 1995

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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