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Related Experiment Videos

PERspective on PER phosphorylation.

Justin Blau1

  • 1Department of Biology, New York University, New York, New York 10003, USA. justin.blau@nyu.edu

Genes & Development
|July 3, 2008
PubMed
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Researchers identified a key phosphorylation site on Period (PER) proteins. This site recruits the F-box protein Slimb, triggering PER degradation and regulating the speed of circadian clocks.

Area of Science:

  • Chronobiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Circadian rhythms are regulated by molecular clocks involving Period (PER) proteins.
  • PER protein stability and localization are controlled by phosphorylation.
  • Identifying key phosphorylation sites on PER has been challenging.

Purpose of the Study:

  • To identify a critical phosphorylation site on Period (PER) proteins.
  • To understand how this site influences PER protein degradation.
  • To elucidate the mechanism for setting circadian clock speed.

Main Methods:

  • Utilized biochemical assays to investigate PER protein phosphorylation.
  • Employed techniques to identify protein-protein interactions involving PER.

Related Experiment Videos

  • Analyzed the role of specific phosphorylation sites in PER degradation pathways.

    • Main Results:

    • Identified a specific phosphorylation site on PER proteins.
    • Demonstrated that this site recruits the F-box protein Slimb.
    • Showed that Slimb recruitment leads to PER degradation, thereby regulating clock speed.

    Conclusions:

    • A key phosphorylation site on PER proteins dictates its stability and degradation.
    • This phosphorylation event is crucial for the timely removal of PER, setting the pace of the circadian clock.
    • Findings provide a molecular mechanism for circadian timekeeping in flies and mammals.