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dc.contributor.authorKasioulis, Ioannis
dc.contributor.authorSyred, Heather M.
dc.contributor.authorTate, Peri
dc.contributor.authorFinch, Andrew
dc.contributor.authorShaw, Joseph
dc.contributor.authorSeawright, Anne
dc.contributor.authorFuszard, Matthew Alexander
dc.contributor.authorBotting, Catherine H.
dc.contributor.authorShirran, Sally
dc.contributor.authorAdams, Ian R.
dc.contributor.authorJackson, Ian J.
dc.contributor.authorvan Heyningen, Veronica
dc.contributor.authorYeyati, Patricia L.
dc.date.accessioned2014-09-04T11:31:02Z
dc.date.available2014-09-04T11:31:02Z
dc.date.issued2014-04-15
dc.identifier145704896
dc.identifiere85588f7-17a1-48a7-99c1-68a46154e61b
dc.identifier000339649400003
dc.identifier84922782912
dc.identifier000339649400003
dc.identifier.citationKasioulis , I , Syred , H M , Tate , P , Finch , A , Shaw , J , Seawright , A , Fuszard , M A , Botting , C H , Shirran , S , Adams , I R , Jackson , I J , van Heyningen , V & Yeyati , P L 2014 , ' Kdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesis ' , Molecular Biology of the Cell , vol. 25 , no. 8 , pp. 1216-1233 . https://doi.org/10.1091/mbc.E13-08-0471en
dc.identifier.issn1059-1524
dc.identifier.otherORCID: /0000-0003-3516-3507/work/32169112
dc.identifier.urihttps://hdl.handle.net/10023/5344
dc.description.abstractThe lysine demethylase Kdm3a (Jhdm2a, Jmjd1a) is required for male fertility, sex determination, and metabolic homeostasis through its nuclear role in chromatin remodeling. Many histone-modifying enzymes have additional nonhistone substrates, as well as nonenzymatic functions, contributing to the full spectrum of events underlying their biological roles. We present two Kdm3a mouse models that exhibit cytoplasmic defects that may account in part for the globozoospermia phenotype reported previously. Electron microscopy revealed abnormal acrosome and manchette and the absence of implantation fossa at the caudal end of the nucleus in mice without Kdm3a demethylase activity, which affected cytoplasmic structures required to elongate the sperm head. We describe an enzymatically active new Kdm3a isoform and show that subcellular distribution, protein levels, and lysine demethylation activity of Kdm3a depended on Hsp90. We show that Kdm3a localizes to cytoplasmic structures of maturing spermatids affected in Kdm3a mutant mice, which in turn display altered fractionation of beta-actin and gamma-tubulin. Kdm3a is therefore a multifunctional Hsp90 client protein that participates directly in the regulation of cytoskeletal components.
dc.format.extent18
dc.format.extent13641283
dc.language.isoeng
dc.relation.ispartofMolecular Biology of the Cellen
dc.subjectHistone demethylaseen
dc.subjectGene-expressionen
dc.subjectIn-vivoen
dc.subjectEpigenetic regulationen
dc.subjectCell-proliferationen
dc.subjectSpermatid headen
dc.subjectStem-cellsen
dc.subjectJmjd1aen
dc.subjectActinen
dc.subjectJhdm2aen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.titleKdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesisen
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.identifier.doihttps://doi.org/10.1091/mbc.E13-08-0471
dc.description.statusPeer revieweden


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