Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation
Open accessAbstract
The SMRT (Silencing Mediator of Retinoid and Thyroid hormone receptors) corepressor mediates gene repression by nuclear receptors and other transcriptional factors. The SMRT protein serves as a key nucleating core that organizes the assembly of a larger corepressor complex. We report here that SMRT interacts with itself to form a protein dimer, and that Erk2, a mitogen-activated protein (MAP) kinase, disrupts this SMRT self-dimerization in vitro and in vivo. Notably Erk2 phosphorylation also results in a re-organization of the overall corepressor complex, characterized by a reduced sedimentation coefficient, partial release of HDAC3, TBL-1, and TBLR-1, and inhibition of transcriptional repression. We propose that SMRT dimers form the central platform on which additional corepressor components assemble, and that kinase signaling modifies the architecture, composition, and function of this complex. These observations contribute to our understanding of how the SMRT corepressor complex assembles and is regulated during cell proliferation and differentiation.
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Phosphorylation of SMRT induces its release from RARs and/or disturbs the organization of the overall corepressor complex.
“This is exemplifi ed by the phosphorylation of SMRT, which induces its release from RARs and/or disturbs the organization of the overall corepressor complex ( 146, 147 ).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [146]
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- Authors
- Varlakhanova, N., Hahm, J. B., & Privalsky, M. L.
- Affiliations
- University of California, Davis (US)
- Corresponding author
- Privalsky, Martin L.
- Venue
- Molecular and Cellular Endocrinology
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 332
- Issue
- 1-2
- Pages
- 180-188
- ISSN
- 0303-7207 (ISSN-L)
- PMC
- PMC3011023
- OpenAlex
- W2061319093
- Cited by
- 24
- References
- 55
- Citations by year
- 2025: 1 · 2023: 1 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 2 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 1
- FWCI
- 1.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Public Health Service/National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- SMRT corepressor, protein dimerization, ERK2, MAPK phosphorylation, HDAC3, transcriptional repression, nuclear receptor corepressor
- MeSH terms
- Animals, Humans, Phosphorylation, Recombinant Fusion Proteins, Signal Transduction, Dimerization, Mitogen-Activated Protein Kinase 1, Protein Structure, Quaternary, Mitogen-Activated Protein Kinases, Multiprotein Complexes, Nuclear Receptor Co-Repressor 2
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