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Targets of the cyclin-dependent kinase Cdk1

Author

Listed:
  • Jeffrey A. Ubersax

    (University of California
    Biophysics, University of California)

  • Erika L. Woodbury

    (University of California
    Biophysics, University of California)

  • Phuong N. Quang

    (University of California
    Biophysics, University of California)

  • Maria Paraz

    (University of California
    Biophysics, University of California)

  • Justin D. Blethrow

    (University of California
    Biophysics, University of California
    University of California)

  • Kavita Shah

    (Genomics Institute of the Novartis Foundation)

  • Kevan M. Shokat

    (University of California)

  • David O. Morgan

    (University of California
    Biophysics, University of California)

Abstract

The events of cell reproduction are governed by oscillations in the activities of cyclin-dependent kinases (Cdks)1. Cdks control the cell cycle by catalysing the transfer of phosphate from ATP to specific protein substrates. Despite their importance in cell-cycle control, few Cdk substrates have been identified2. Here, we screened a budding yeast proteomic library for proteins that are directly phosphorylated by Cdk1 in whole-cell extracts. We identified about 200 Cdk1 substrates, several of which are phosphorylated in vivo in a Cdk1-dependent manner. The identities of these substrates reveal that Cdk1 employs a global regulatory strategy involving phosphorylation of other regulatory molecules as well as phosphorylation of the molecular machines that drive cell-cycle events. Detailed analysis of these substrates is likely to yield important insights into cell-cycle regulation.

Suggested Citation

  • Jeffrey A. Ubersax & Erika L. Woodbury & Phuong N. Quang & Maria Paraz & Justin D. Blethrow & Kavita Shah & Kevan M. Shokat & David O. Morgan, 2003. "Targets of the cyclin-dependent kinase Cdk1," Nature, Nature, vol. 425(6960), pages 859-864, October.
    • Handle: RePEc:nat:nature:v:425:y:2003:i:6960:d:10.1038_nature02062
    DOI: 10.1038/nature02062
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    Cited by:

    1. Juan Manuel Valverde & Geronimo Dubra & Michael Phillips & Austin Haider & Carlos Elena-Real & Aurélie Fournet & Emile Alghoul & Dhanvantri Chahar & Nuria Andrés-Sanchez & Matteo Paloni & Pau Bernadó , 2023. "A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation," Nature Communications, Nature, vol. 14(1), pages 1-23, December.
    2. Emily N Manderson & Mohan Malleshaiah & Stephen W Michnick, 2008. "A Novel Genetic Screen Implicates Elm1 in the Inactivation of the Yeast Transcription Factor SBF," PLOS ONE, Public Library of Science, vol. 3(1), pages 1-9, January.
    3. Michelle M. Conti & Rui Li & Michelle A. Narváez Ramos & Lihua Julie Zhu & Thomas G. Fazzio & Jennifer A. Benanti, 2023. "Phosphosite Scanning reveals a complex phosphorylation code underlying CDK-dependent activation of Hcm1," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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