A novel role for protein arginine deiminase 4 in pluripotency: The emerging role of citrullinated histone H1 in cellular programming

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dc.contributor.authorSlade, Daniel J.en
dc.contributor.authorHoribata, Sachien
dc.contributor.authorCoonrod, Scott A.en
dc.contributor.authorThompson, Paul R.en
dc.contributor.departmentBiochemistryen
dc.contributor.departmentCenter for Drug Discoveryen
dc.date.accessioned2016-11-09T03:12:55Zen
dc.date.available2016-11-09T03:12:55Zen
dc.date.issued2014-08en
dc.description.abstractHistone post-translational modifications (PTM) alter the chromatin architecture, generating ‘open’ and ‘closed’ states, and these structural changes can modulate gene expression under specific cellular conditions. While methylation and acetylation are the best-characterized histone PTMs, citrullination by the protein arginine deiminases (PADs) represents another important player in this process. In addition to “fine tuning” chromatin structure at specific loci, histone citrullination can also promote rapid global chromatin decondensation during the formation of extracellular traps (ETs) in immune cells. Recent studies now show that PAD4-mediated citrullination of histone H1 at promoter elements can also promote localized chromatin decondensation in stem cells, thus regulating the pluripotent state. These observations suggest that PAD-mediated histone deimination profoundly affects chromatin structure, possibly above and beyond that of other PTMs. Additionally, these recent findings further enhance our understanding of PAD biology and the important contributions that these enzymes play in development, health, and disease.en
dc.description.versionPublished versionen
dc.format.extent736 - 740 page(s)en
dc.identifier.doihttps://doi.org/10.1002/bies.201400057en
dc.identifier.issn0265-9247en
dc.identifier.issue8en
dc.identifier.urihttp://hdl.handle.net/10919/73407en
dc.identifier.volume36en
dc.language.isoenen
dc.relation.urihttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000339551700005&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=930d57c9ac61a043676db62af60056c1en
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectcanceren
dc.subjectchromatinen
dc.subjectdeiminaseen
dc.subjectgene regulationen
dc.subjecthistoneen
dc.subjectpluripotencyen
dc.subjectrheumatoid arthritisen
dc.subjectstem cellsen
dc.titleA novel role for protein arginine deiminase 4 in pluripotency: The emerging role of citrullinated histone H1 in cellular programmingen
dc.title.serialBioessaysen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten
pubs.organisational-group/Virginia Techen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciencesen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/Biochemistryen
pubs.organisational-group/Virginia Tech/Agriculture & Life Sciences/CALS T&R Facultyen
pubs.organisational-group/Virginia Tech/All T&R Facultyen
pubs.organisational-group/Virginia Tech/Faculty of Health Sciencesen

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