Heterodimerization of E proteins with Myod

Stable Identifier
Reaction [binding]
Mus musculus
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Heterodimerization of E proteins with Myod

MyoD is a basic helix loop helix (bHLH) myoblast specific transcription factor defined as a 'master switch' gene in that it can convert other cell types into muscles if the gene is active in them. bHLH proteins Myf5, Myogenin and MRF4/Myf6 are highly related to MyoD and these along with MyoD form the 'MyoD family' of transcription factors, also called the myogenic regulatory factors (MRFs).
MRFs form transcriptionally active heterodimers with the widely expressed E proteins, a distinct group of bHLH proteins including E12/E47, ITF-2 and HEB. Dimerization of these proteins juxtaposes their basic domains forming a functional DNA binding domain. MyoD/E protein heterodimers preferentially bind the DNA consensus sequence referred to as an E-box (CANNTG) in the control regions of muscle-specific genes and activate gene transcription of genes that are expressed in skeletal muscle.

Literature References
PubMed ID Title Journal Year
15719023 E47 phosphorylation by p38 MAPK promotes MyoD/E47 association and muscle-specific gene transcription

Lluis, F, Ballestar, E, Suelves, M, Esteller, M, Muñoz-Cánoves, P

EMBO J 2005
2503252 Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence

Murre, C, McCaw, PS, Vaessin, H, Caudy, M, Jan, LY, Jan, YN, Cabrera, CV, Buskin, JN, Hauschka, SD, Lassar, AB

Cell 1989
1649701 Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo

Lassar, AB, Davis, RL, Wright, WE, Kadesch, T, Murre, C, Voronova, A, Baltimore, D, Weintraub, H

Cell 1991
Orthologous Events
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