Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation
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...
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Published in | Molecular and cellular endocrinology Vol. 332; no. 1-2; pp. 180 - 188 |
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Format | Journal Article |
Language | English |
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30.01.2011
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Abstract | 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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AbstractList | 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. 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. |
Author | Privalsky, Martin L. Hahm, Johnnie B. Varlakhanova, Natalia |
AuthorAffiliation | 1 Department of Microbiology College of Biological Sciences University of California at Davis 2 Currently at the Department of Cell and Human Anatomy College of Medicine University of California at Davis |
AuthorAffiliation_xml | – name: 2 Currently at the Department of Cell and Human Anatomy College of Medicine University of California at Davis – name: 1 Department of Microbiology College of Biological Sciences University of California at Davis |
Author_xml | – sequence: 1 givenname: Natalia surname: Varlakhanova fullname: Varlakhanova, Natalia – sequence: 2 givenname: Johnnie B. surname: Hahm fullname: Hahm, Johnnie B. – sequence: 3 givenname: Martin L. surname: Privalsky fullname: Privalsky, Martin L. email: mlprivalsky@ucdavis.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20965228$$D View this record in MEDLINE/PubMed |
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Snippet | The SMRT (Silencing Mediator of Retinoid and Thyroid hormone receptors) corepressor mediates gene repression by nuclear receptors and other transcriptional... |
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SubjectTerms | Animals Architecture cell proliferation Corepressor complex Dimer Dimerization Erk genes Humans MAP kinases mitogen-activated protein kinase Mitogen-Activated Protein Kinase 1 - genetics Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinases - metabolism Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Nuclear Receptor Co-Repressor 2 - chemistry Nuclear Receptor Co-Repressor 2 - genetics Nuclear Receptor Co-Repressor 2 - metabolism Phosphorylation Protein Structure, Quaternary Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Signal Transduction SMRT thyroid hormone receptors transcription (genetics) transcription factors |
Title | Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation |
URI | https://dx.doi.org/10.1016/j.mce.2010.10.010 https://www.ncbi.nlm.nih.gov/pubmed/20965228 https://search.proquest.com/docview/821597753 https://search.proquest.com/docview/855709594 https://pubmed.ncbi.nlm.nih.gov/PMC3011023 |
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