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CLOCK-mediated acetylation of BMAL1 controls circadian function

CLOCK, a protein that regulates circadian rhythm, also acetylates its partner protein, BMAL1 on a unique, highly conserved Lys 537 residue, as a recent study by Jun Hirayama from the University of California (USA) shows.
CLOCK, a protein that regulates circadian rhythm, also acetylates its partner protein, BMAL1 on a unique, highly conserved Lys 537 residue, as a recent study by Jun Hirayama from the University of California (USA) shows.

The CLOCK-BMAL1 complex is responsible for activating CLOCK-controlled genes, like cryptochromes (Crys). The gene products directly repress CLOCK-BMAL1.

The scientists discovered that BMAL1 undergoes rhythmic acetylation in murine liver tissue. The timing was observed to parallel the circadian transcriptional downregulation of CLOCK-controlled genes. The BMAL1 acetylation supports transcriptional repression by facilitating the recruitment of CRY1 to CLOCK-BMAL1 complexes.

Ectopic expression of mutated BMAL1 (K537R-mutation) cannot rescue circadian rhythmicity in vitro. The circadian machinery therefore requires the enzymatic interaction of two CLOCK core components.

Related antibodies on antibodies-online.com:

CLOCK

BMAL1

Cryptochrome (CRY)

Cryptochrome 1 (CRY1)

CLOCK (mouse homolog)

CLOCK (drosophila)

Cryptochrome (drosophila)

Cryptochrome 1 (mouse)

29.01.2008  |  Anna Lena Marwedel      RSS Feed  Research News


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