Prediction of Cyclin-Dependent Kinase Phosphorylation Substrates CDK Substrate Prediction Model
2007

Predicting Cyclin-Dependent Kinase Phosphorylation Substrates

Sample size: 91 publication Evidence: moderate

Author Information

Author(s): Chang Emmanuel J., Begum Rashida, Chait Brian T., Gaasterland Terry

Primary Institution: Department of Chemistry, York College of the City University of New York

Hypothesis

Cdk substrates might contain clusters of phosphorylation sites, and therefore that Cdk substrate prediction could be improved by optimizing the consensus motif sequence and selecting proteins whose sequences are enriched for repeats of that motif.

Conclusion

The study presents a model for predicting Cdk substrates that incorporates both local and global sequence characteristics, successfully identifying a significant number of putative substrates.

Supporting Evidence

  • The model predicts a set of 91 candidate Cdk substrate proteins comprising 1.5% of the yeast proteome.
  • 46 of the candidate substrates were defined as strong candidates, detected using the canonical-motif scoring method.
  • 22 of the 35 candidates matched the top scoring in vitro substrates.
  • Many of the candidate substrates were also predicted to contain Cdk phosphorylation sites using other leading phosphorylation detection algorithms.

Takeaway

The researchers created a computer program to find proteins that can be changed by a special process called phosphorylation, which helps cells divide properly.

Methodology

The study used a computational procedure to model Cdk substrates based on both local and global characteristics of the substrates, incorporating clustering of phosphorylation sites.

Potential Biases

The known set of phosphorylation sites for a particular kinase may be systematically biased, potentially leading to false negatives.

Limitations

The method may miss certain known substrates and is less comprehensive, yielding a set of likely candidate substrates rather than a complete list.

Digital Object Identifier (DOI)

10.1371/journal.pone.0000656

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