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dc.contributor.authorEe, Ly-Sha
dc.contributor.authorMcCannell, Kurtis N.
dc.contributor.authorTang, Yang
dc.contributor.authorFernandes, Nancy
dc.contributor.authorHardy, W. Rod
dc.contributor.authorGreen, Michael R.
dc.contributor.authorChu, Feixia
dc.contributor.authorFazzio, Thomas G.
dc.date2022-08-11T08:09:47.000
dc.date.accessioned2022-08-23T16:43:41Z
dc.date.available2022-08-23T16:43:41Z
dc.date.issued2017-06-06
dc.date.submitted2017-10-11
dc.identifier.citationStem Cell Reports. 2017 Jun 6;8(6):1488-1496. doi: 10.1016/j.stemcr.2017.04.020. Epub 2017 May 18. <a href="https://doi.org/10.1016/j.stemcr.2017.04.020">Link to article on publisher's site</a>
dc.identifier.issn2213-6711 (Linking)
dc.identifier.doi10.1016/j.stemcr.2017.04.020
dc.identifier.pmid28528697
dc.identifier.urihttp://hdl.handle.net/20.500.14038/40348
dc.description<p>First author Ly-Sha Ee is a doctoral student in the Interdisciplinary Graduate Program in the Graduate School of Biomedical Sciences (GSBS) at UMass Medical School.</p>
dc.description.abstractThe Nucleosome Remodeling and Deacetylase (NuRD) complex is a chromatin regulatory complex that functions as a transcriptional co-repressor in metazoans. The NuRD subunit MBD3 is essential for targeting and assembly of a functional NuRD complex as well as embryonic stem cell (ESC) pluripotency. Three MBD3 isoforms (MBD3A, MBD3B, and MBD3C) are expressed in mouse. Here, we find that the MBD3C isoform contains a unique 50-amino-acid N-terminal region that is necessary for MBD3C to specifically interact with the histone H3 binding protein WDR5. Domain analyses of WDR5 reveal that the H3 binding pocket is required for interaction with MBD3C. We find that while Mbd3c knockout ESCs differentiate normally, MBD3C is redundant with the MBD3A and MBD3B isoforms in regulation of gene expression, with the unique MBD3C N terminus required for this redundancy. Together, our data characterize a unique NuRD complex variant that functions specifically in ESCs.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=28528697&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 2017 The Author(s)
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectMbd3
dc.subjectNuRD
dc.subjectWdr5
dc.subjectchromatin
dc.subjectdifferentiation
dc.subjectCancer Biology
dc.subjectCell Biology
dc.subjectMolecular Biology
dc.titleAn Embryonic Stem Cell-Specific NuRD Complex Functions through Interaction with WDR5
dc.typeJournal Article
dc.source.journaltitleStem cell reports
dc.source.volume8
dc.source.issue6
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=4155&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/3147
dc.identifier.contextkey10887403
refterms.dateFOA2022-08-23T16:43:41Z
html.description.abstract<p>The Nucleosome Remodeling and Deacetylase (NuRD) complex is a chromatin regulatory complex that functions as a transcriptional co-repressor in metazoans. The NuRD subunit MBD3 is essential for targeting and assembly of a functional NuRD complex as well as embryonic stem cell (ESC) pluripotency. Three MBD3 isoforms (MBD3A, MBD3B, and MBD3C) are expressed in mouse. Here, we find that the MBD3C isoform contains a unique 50-amino-acid N-terminal region that is necessary for MBD3C to specifically interact with the histone H3 binding protein WDR5. Domain analyses of WDR5 reveal that the H3 binding pocket is required for interaction with MBD3C. We find that while Mbd3c knockout ESCs differentiate normally, MBD3C is redundant with the MBD3A and MBD3B isoforms in regulation of gene expression, with the unique MBD3C N terminus required for this redundancy. Together, our data characterize a unique NuRD complex variant that functions specifically in ESCs.</p>
dc.identifier.submissionpathoapubs/3147
dc.contributor.departmentGraduate School of Biomedical Sciences, Interdisciplinary Graduate Program
dc.contributor.departmentDepartment of Molecular, Cell, and Cancer Biology
dc.source.pages1488-1496


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