Targeted proteomic study of the cyclin-Cdk module

Vincent Archambault, Emmanuel J. Chang, Benjamin J. Drapkin, Frederick R. Cross, Brian T. Chait, Michael P. Rout

Research output: Contribution to journalArticlepeer-review

94 Scopus citations


The cell division cycle of the yeast S. cerevisiae is driven by one Cdk (cyclin-dependent kinase), which becomes active when bound to one of nine cyclin subunits. Elucidation of Cdk substrates and other Cdk-associated proteins is essential for a full understanding of the cell cycle. Here, we report the results of a targeted proteomics study using affinity purification coupled to mass spectrometry. Our study identified numerous proteins in association with particular cyclin-Cdk complexes. These included phosphorylation substrates, ubiquitination-degradation proteins, adaptors, and inhibitors. Some associations were previously known, and for others, we confirmed their specificity and biological relevance. Using a hypothesis-driven mass spectrometric approach, we also mapped in vivo phosphorylation at Cdk consensus motif-containing peptides within several cyclin-associated candidate Cdk substrates. Our results demonstrate that this approach can be used to detect a host of transient and dynamic protein associations within a biological module.

Original languageEnglish (US)
Pages (from-to)699-711
Number of pages13
JournalMolecular cell
Issue number6
StatePublished - Jun 18 2004
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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