Bmal1 binds Clock,Npas2 forming Bmal1:Clock,Npas2 heterodimer

Stable Identifier
Reaction [binding]
Mus musculus
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Bmal1 binds Clock,Npas2 forming Bmal1:Clock,Npas2 heterodimer

Bmal1 (Arntl), Clock, and Npas2 are basic helix-loop-helix transcription factors. Bmal1 can form a heterodimer with either Clock or Npas2. By analogy with other basic helix-loop-helix proteins the basic domain probably binds DNA, in this case the E-box motif, and the helix-loop-helix domains interact to form the heterodimer. Bmal1 and Clock/Npas2 are codependently phosphorylated by unknown kinases after dimerization. The phosphorylation enhances transactivation activity and is inhibited by Per:Cry complexes. Both Clock and Npas2 are expressed in the suprachiasmatic nucleus of the hypothalamus and act redundantly there. The tissue distributions of Clock and Npas2 do not entirely overlap, however. For example, Npas2 but not Clock is found in forebrain.

Literature References
PubMed ID Title Journal Year
17417633 CLOCK and NPAS2 have overlapping roles in the suprachiasmatic circadian clock

Reppert, SM, DeBruyne, JP, Weaver, DR

Nat Neurosci 2007
18316400 Evidence for an overlapping role of CLOCK and NPAS2 transcription factors in liver circadian oscillators

FoĆ”, A, Tosini, G, Caruso, P, Cavallari, N, Bertolucci, C, Bernardi, F, Colognesi, I, Pinotti, M, Aguzzi, J, Chen, Z

Mol Cell Biol 2008
9616112 Role of the CLOCK protein in the mammalian circadian mechanism

King, DP, Nguyen, HB, Weitz, CJ, Takahashi, JS, Staknis, D, Gekakis, N, Davis, FC, Wilsbacher, LD

Science 1998
17115977 Cryptochromes impair phosphorylation of transcriptional activators in the clock: a general mechanism for circadian repression

Fortier, EE, Cermakian, N, Martineau, V, Dardente, H

Biochem J 2007
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