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Parallel Measurement of Circadian Clock Gene Expression and Hormone Secretion in Human Primary Cell Cultures
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CLOCK-mediated acetylation of BMAL1 controls circadian function.

Jun Hirayama1, Saurabh Sahar, Benedetto Grimaldi

  • 1Department of Pharmacology, School of Medicine, University of California Irvine, Irvine 92697-4625, California, USA.

Nature
|December 14, 2007
PubMed
Summary

The CLOCK protein acetylates its partner BMAL1, a key step in regulating the body's internal clock. This acetylation is crucial for the proper functioning of circadian rhythms and gene expression.

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Area of Science:

  • Molecular Biology
  • Chronobiology
  • Epigenetics

Background:

  • Circadian rhythms are regulated by transcriptional-translational feedback loops.
  • The CLOCK-BMAL1 complex activates gene expression, while cryptochromes (Crys) repress it.
  • CLOCK has intrinsic histone acetyltransferase activity influencing gene expression.

Purpose of the Study:

  • To investigate the non-histone acetylation activity of CLOCK.
  • To determine the role of BMAL1 acetylation in circadian rhythm regulation.

Main Methods:

  • Analysis of BMAL1 acetylation in mouse liver.
  • Mutation of the conserved Lysine 537 residue in BMAL1.
  • Cellular models to assess circadian rhythmicity rescue.

Main Results:

  • CLOCK directly acetylates BMAL1 on Lysine 537.
  • BMAL1 acetylation is rhythmic and occurs in mouse liver.
  • Acetylated BMAL1 enhances CRY1 recruitment, promoting transcriptional repression.
  • A K537R-mutated BMAL1 fails to restore circadian rhythmicity.

Conclusions:

  • CLOCK-BMAL1 enzymatic interplay is essential for circadian machinery.
  • BMAL1 acetylation by CLOCK is a critical regulatory mechanism.
  • This post-translational modification fine-tunes circadian gene expression.