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

Andrew B. Lassar, Robert L. Davis, Woodring E. Wright, Tom Kadesch, Cornelis Murre, Anna Voronova, David Baltimore, Harold Weintraub

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662 Scopus citations

Abstract

In this report we provide four lines of evidence indicating that E12/E47-like proteins interact in vivo with the myogenic HLH proteins MyoD and myogenin. First, cotransfection of MyoD and E47 in COS cells indicates that these factors synergistically enhance transcription of a reporter gene containing an oligomerized MyoD-binding site. Second, mobility-shift assays of muscle cell nuclear extracts, "double shifted" with specific antisera, have identified complexes binding to the MEF1 site that contain either MyoD or myogenin in association with El 2/E47-like proteins. Third, association with E47 alters the phosphorylation state of MyoD. Fourth, C3H10T1/2 cells expressing antisense E2A transcripts contain low levels of E2A gene products and display less terminal muscle differentiation when infected with retroviral MyoD or when challenged to differentiate with 5-azacytidine treatment. In addition we demonstrate that MyoD, in conjunction with E12/E47-like proteins, is functioning as a regulatory nodal point for activation of several other downstream muscle regulators.

Original languageEnglish (US)
Pages (from-to)305-315
Number of pages11
JournalCell
Volume66
Issue number2
DOIs
StatePublished - Jul 26 1991

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Lassar, A. B., Davis, R. L., Wright, W. E., Kadesch, T., Murre, C., Voronova, A., Baltimore, D., & Weintraub, H. (1991). Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. Cell, 66(2), 305-315. https://doi.org/10.1016/0092-8674(91)90620-E