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Cited by 518

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases

Open access
Lu, Jianrong, McKinsey, Timothy A., Nicol, Rebekka L., Olson, Eric N.·2000·Proceedings of the National Academy of Sciences

Abstract

Myocyte enhancer factor-2 (MEF2) transcription factors control muscle-specific and growth factor-inducible genes. We show that hypertrophic growth of cardiomyocytes in response to phenylephrine and serum is accompanied by activation of MEF2 through a posttranslational mechanism mediated by calcium, calmodulin-dependent protein kinase (CaMK), and mitogen-activated protein kinase (MAPK) signaling. CaMK stimulates MEF2 activity by dissociating class II histone deacetylases (HDACs) from the DNA-binding domain. MAPKs, which activate MEF2 by phosphorylation of the transcription activation domain, maximally stimulate MEF2 activity only when repression by HDACs is relieved by CaMK signaling to the DNA-binding domain. These findings identify MEF2 as an endpoint for hypertrophic stimuli in cardiomyocytes and demonstrate that MEF2 mediates synergistic transcriptional responses to the CaMK and MAPK signaling pathways by signal-dependent dissociation from HDACs.

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Metadata

Authors
Lu, J., McKinsey, T. A., Nicol, R. L., & Olson, E. N.
Venue
Proceedings of the National Academy of Sciences
Published
2000-03-28
Volume
97
Issue
8
Pages
4070-4075
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2117813626
Cited by
518
References
3
FWCI
11.04
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. https://app.cochat.ai/papers/10.1073/pnas.080064097
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Lu, J., McKinsey, T. A., Nicol, R. L., & Olson, E. N. (2000). Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.080064097

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