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PSMD11 modulates circadian clock function through PER and CRY nuclear translocation.

Sibel Cal-Kayitmazbatir1, Lauren J Francey1, Yool Lee2,3

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The NRON complex component PSMD11 regulates circadian clock proteins PER2 and CRY2 stability and CRY1 nuclear translocation, maintaining cellular circadian rhythms.

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Area of Science:

  • Molecular Biology
  • Chronobiology
  • Cellular Biology

Background:

  • The molecular circadian clock relies on transcriptional-translational feedback loops.
  • Post-translational regulation of the circadian clock, particularly by large ribonucleoprotein complexes like NRON, is not well understood.
  • PSMD11, a component of the NRON complex and the 26S proteasome, shows specific involvement in circadian clock function.

Purpose of the Study:

  • To investigate the role of PSMD11 within the NRON complex in regulating the stability and nuclear translocation of circadian clock proteins.
  • To elucidate the specific mechanisms by which PSMD11 influences circadian rhythmicity at the molecular level.

Main Methods:

  • Utilized cell-based and biochemical approaches to study PSMD11 function.
  • Employed size exclusion chromatography for enrichment of the NRON complex in cytosolic and nuclear fractions.
  • Performed PSMD11 knockdown experiments to assess effects on circadian protein levels and localization.

Main Results:

  • PSMD11 knockdown altered the abundance of PER2 and CRY2 proteins.
  • Knockdown of PSMD11 impaired the nuclear translocation of CRY1, altering the nuclear ratio of CRY1 and CRY2.
  • Characterized PSMD11's role in regulating the stability and nuclear entry of key circadian repressors.

Conclusions:

  • PSMD11 plays a crucial role in the NRON complex by governing the nuclear translocation of circadian repressors.
  • This regulation by PSMD11 is essential for the proper functioning and maintenance of cellular circadian oscillations.
  • Highlights the importance of post-translational modifications and protein complex interactions in circadian clock regulation.