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http://purl.uniprot.org/citations/18374647http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18374647http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18374647http://www.w3.org/2000/01/rdf-schema#comment"SUMOylation is essential for cell-cycle regulation in invertebrates; however, its functions during the mammalian cell cycle are largely uncharacterized. Mammals express three SUMO paralogs: SUMO-1, SUMO-2, and SUMO-3 (SUMO-2 and SUMO-3 are 96% identical and referred to as SUMO-2/3). We found that SUMO-2/3 localize to centromeres and condensed chromosomes, whereas SUMO-1 localizes to the mitotic spindle and spindle midzone, indicating that SUMO paralogs regulate distinct mitotic processes in mammalian cells. Consistent with this, global inhibition of SUMOylation caused a prometaphase arrest due to defects in targeting the microtubule motor protein CENP-E to kinetochores. CENP-E was found to be modified specifically by SUMO-2/3 and to possess SUMO-2/3 polymeric chain-binding activity essential for kinetochore localization. Our findings indicate that SUMOylation is a key regulator of the mammalian cell cycle, with SUMO-1 and SUMO-2/3 modification of different proteins regulating distinct processes."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.01.013"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.01.013"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Porter A.C.G."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Porter A.C.G."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Matunis M.J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Matunis M.J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Yen T.J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Yen T.J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Goeres J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Goeres J."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Zhang X.-D."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/author"Zhang X.-D."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/pages"729-741"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/pages"729-741"xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/title"SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis."xsd:string
http://purl.uniprot.org/citations/18374647http://purl.uniprot.org/core/title"SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis."xsd:string