Targeted proteomic study of the cyclin-Cdk module.

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.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Cell Cycle Proteins, Cyclin B, Cyclin-Dependent Kinases, Cyclins, DNA-Binding Proteins, Mass Spectrometry, Molecular Sequence Data, Phosphorylation, Proteomics, Saccharomyces cerevisiae Proteins, Transcription Factors, Ubiquitins
Mol. Cell
Date: Jun. 18, 2004
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