MEF‐2 function is modified by a novel co‐repressor, MITR

Sparrow, Duncan B.; Miska, Eric A.; Langley, Emma; Reynaud‐Deonauth, Sorogini; Kotecha, Surendra; Towers, Norma; Spohr, Georges; Kouzarides, Tony; Mohun, Timothy J.

doi:10.1093/emboj/18.18.5085

Cited by 196Genomics and Chromatin DynamicsDevelopmental Biology and Gene RegulationMuscle Physiology and Disorders

MEF‐2 function is modified by a novel co‐repressor, MITR

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Sparrow, Duncan B., Miska, Eric A., Langley, Emma, Reynaud‐Deonauth, Sorogini, Kotecha, Surendra, Towers, Norma, Spohr, Georges, Kouzarides, Tony +1 more·1999·The EMBO Journal

DOI 10.1093/emboj/18.18.5085PMC PMC1171579

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Abstract

The MEF-2 proteins are a family of transcriptional activators that have been detected in a wide variety of cell types. In skeletal muscle cells, MEF-2 proteins interact with members of the MyoD family of transcriptional activators to synergistically activate gene expression. Similar interactions with tissue or lineage-specific cofactors may also underlie MEF-2 function in other cell types. In order to screen for such cofactors, we have used a transcriptionally inactive mutant of Xenopus MEF2D in a yeast two-hybrid screen. This approach has identified a novel protein expressed in the early embryo that binds to XMEF2D and XMEF2A. The MEF-2 interacting transcription repressor (MITR) protein binds to the N-terminal MADS/MEF-2 region of the MEF-2 proteins but does not bind to the related Xenopus MADS protein serum response factor. In the early embryo, MITR expression commences at the neurula stage within the mature somites and is subsequently restricted to the myotomal muscle. In functional assays, MITR negatively regulates MEF-2-dependent transcription and we show that this repression is mediated by direct binding of MITR to the histone deacetylase HDAC1. Thus, we propose that MITR acts as a co-repressor, recruiting a specific deacetylase to downregulate MEF-2 activity.

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A natural HDAC9 splice variant lacking the HDAC domain (MITR/HDRP) and analogous artificially truncated forms of other class IIa members retain full transcriptional repressive functions.
“A natural HDAC9 splice variant lacking the HDAC domain [myocyte enhancer factor-2 interacting transcription repressor/HDAC-related protein (MITR/HDRP)] as well as analogous artificially truncated forms of other class IIa members retain full transcriptional repressive functions (16,17).”
From Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases (2007) · cites this paper as [17]

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Cellular levels of the prophage λ and 434 repressors
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Authors: Sparrow, D. B., Miska, E. A., Langley, E., Reynaud‐Deonauth, S., Kotecha, S., Towers, N., Spohr, G., Kouzarides, T., & Mohun, T. J.
Affiliations: National Institute for Medical Research (GB)
University of Cambridge (GB)
University of Geneva (CH)
Corresponding author: Mohun, Timothy J.
ORCID: Sparrow, Duncan B.
Miska, Eric A.
Kouzarides, Tony
Mohun, Timothy J.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1999-09-15
Volume: 18
Issue: 18
Pages: 5085-5098
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/18.18.5085
PMC: PMC1171579
OpenAlex: W2010466297
Cited by: 196
References: 70
Citations by year: 2025: 3 · 2024: 4 · 2023: 5 · 2022: 1 · 2021: 4 · 2020: 7 · 2019: 2 · 2018: 3 · 2017: 5 · 2016: 8 · 2015: 6 · 2014: 6 · 2013: 1 · 2012: 4
FWCI: 6.79
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Cancer Research Institute
Wellcome Trust
British Heart Foundation
Medical Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Keywords: MEF2, corepressors, transcriptional repression, HDAC1, histone deacetylase, serum response factor, skeletal muscle development, early embryo, somites, myotomal muscle, transcriptional activator
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, DNA-Binding Proteins, Female, Histone Deacetylases, Humans, Molecular Sequence Data, Mutation, Repressor Proteins, Transcription Factors, Xenopus, Transcriptional Activation, Gene Expression, Sequence Homology, Amino Acid, In Situ Hybridization, Myogenic Regulatory Factors, DNA, Complementary, Muscle, Skeletal, Two-Hybrid System Techniques, MADS Domain Proteins, Xenopus Proteins, MEF2 Transcription Factors, In Vitro Techniques

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