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dc.contributor.authorPadilla-Benavides, Teresita
dc.contributor.authorHaokip, Dominic T.
dc.contributor.authorYoon, Yeonsoo
dc.contributor.authorReyes-Gutierrez, Pablo
dc.contributor.authorRivera, Jaime A.
dc.contributor.authorImbalzano, Anthony N.
dc.date2022-08-11T08:09:55.000
dc.date.accessioned2022-08-23T16:48:48Z
dc.date.available2022-08-23T16:48:48Z
dc.date.issued2020-01-30
dc.date.submitted2020-02-18
dc.identifier.citation<p>Padilla-Benavides T, Haokip DT, Yoon Y, Reyes-Gutierrez P, Rivera-Pérez JA, Imbalzano AN. CK2-Dependent Phosphorylation of the Brg1 Chromatin Remodeling Enzyme Occurs during Mitosis. Int J Mol Sci. 2020 Jan 30;21(3):E923. doi: 10.3390/ijms21030923. PMID: 32019271. <a href="https://doi.org/10.3390/ijms21030923">Link to article on publisher's site</a></p>
dc.identifier.issn1422-0067 (Linking)
dc.identifier.doi10.3390/ijms21030923
dc.identifier.pmid32019271
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41336
dc.description.abstractBrg1 (Brahma-related gene 1) is one of two mutually exclusive ATPases that can act as the catalytic subunit of mammalian SWI/SNF (mSWI/SfigureNF) chromatin remodeling enzymes that facilitate utilization of the DNA in eukaryotic cells. Brg1 is a phospho-protein, and its activity is regulated by specific kinases and phosphatases. Previously, we showed that Brg1 interacts with and is phosphorylated by casein kinase 2 (CK2) in a manner that regulates myoblast proliferation. Here, we use biochemical and cell and molecular biology approaches to demonstrate that the Brg1-CK2 interaction occurred during mitosis in embryonic mouse somites and in primary myoblasts derived from satellite cells isolated from mouse skeletal muscle tissue. The interaction of CK2 with Brg1 and the incorporation of a number of other subunits into the mSWI/SNF enzyme complex were independent of CK2 enzymatic activity. CK2-mediated hyperphosphorylation of Brg1 was observed in mitotic cells derived from multiple cell types and organisms, suggesting functional conservation across tissues and species. The mitotically hyperphosphorylated form of Brg1 was localized with soluble chromatin, demonstrating that CK2-mediated phosphorylation of Brg1 is associated with specific partitioning of Brg1 within subcellular compartments. Thus, CK2 acts as a mitotic kinase that regulates Brg1 phosphorylation and subcellular localization.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=32019271&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBrg1
dc.subjectSMARCA4
dc.subjectcasein kinase 2
dc.subjectcell proliferation
dc.subjectchromatin remodeling enzyme
dc.subjectmitosis
dc.subjectmyoblasts
dc.subjectphosphorylation
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry
dc.subjectCell Biology
dc.subjectCells
dc.subjectEnzymes and Coenzymes
dc.subjectMolecular Biology
dc.titleCK2-Dependent Phosphorylation of the Brg1 Chromatin Remodeling Enzyme Occurs during Mitosis
dc.typeJournal Article
dc.source.journaltitleInternational journal of molecular sciences
dc.source.volume21
dc.source.issue3
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=5139&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/4120
dc.identifier.contextkey16574432
refterms.dateFOA2022-08-23T16:48:48Z
html.description.abstract<p>Brg1 (Brahma-related gene 1) is one of two mutually exclusive ATPases that can act as the catalytic subunit of mammalian SWI/SNF (mSWI/SfigureNF) chromatin remodeling enzymes that facilitate utilization of the DNA in eukaryotic cells. Brg1 is a phospho-protein, and its activity is regulated by specific kinases and phosphatases. Previously, we showed that Brg1 interacts with and is phosphorylated by casein kinase 2 (CK2) in a manner that regulates myoblast proliferation. Here, we use biochemical and cell and molecular biology approaches to demonstrate that the Brg1-CK2 interaction occurred during mitosis in embryonic mouse somites and in primary myoblasts derived from satellite cells isolated from mouse skeletal muscle tissue. The interaction of CK2 with Brg1 and the incorporation of a number of other subunits into the mSWI/SNF enzyme complex were independent of CK2 enzymatic activity. CK2-mediated hyperphosphorylation of Brg1 was observed in mitotic cells derived from multiple cell types and organisms, suggesting functional conservation across tissues and species. The mitotically hyperphosphorylated form of Brg1 was localized with soluble chromatin, demonstrating that CK2-mediated phosphorylation of Brg1 is associated with specific partitioning of Brg1 within subcellular compartments. Thus, CK2 acts as a mitotic kinase that regulates Brg1 phosphorylation and subcellular localization.</p>
dc.identifier.submissionpathoapubs/4120
dc.contributor.departmentImbalzano Lab
dc.contributor.departmentDepartment of Pediatrics, Division of Genes and Development
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pagesE923


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© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
Except where otherwise noted, this item's license is described as © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).