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Published July 26, 1991 | public
Journal Article

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

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 E12/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.

Additional Information

© 1991 Published by Elsevier Inc. Received 2 November 1990, Accepted 24 May 1991. We thank Bruce Paterson for SV2-chicken MyoD, Janet Mar and Charles Ordahl for M-CAT oligonucleotides, and our colleagues at the Hutchinson Center for their thoughtful comments and suggestions. This work was supported by grants from the NIH, Howard Hughes Medical Institute, and the Lucille P. Markey Charitable Trust; a portion of this work was supported by Public Health Service grant GM39458 (D. B.). A. B. L. is a Lucille P. Markey Scholar. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC Section 1734 solely to indicate this fact.

Additional details

Created:
August 20, 2023
Modified:
October 20, 2023