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Article: Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization

TitleMitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization
Authors
Issue Date2007
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.html
Citation
Cell Research, 2007, v. 17 n. 5, p. 449-457 How to Cite?
AbstractDuring cell division, chromosome segregation is orchestrated by the interaction of spindle microtubules with the centromere. A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis. Central spindle organization requires mitotic kinesins, the chromosomal passenger protein complex, and microtubule bundling protein PRC1. PRC1 is phosphorylated by Cdc2 at Thr470 and Thr481 during mitosis. However, the functional relevance of PRC1 phosphorylation at Thr470 has remained elusive. Here we show that expression of the non-phosphorylatable mutant PRC1 T470A but not the phospho-mimicking mutant PRC1 T470E causes aberrant organization of the central spindle. Immunoprecipitation experiment indicates that both PRC1 T470A and PRC1 T470E mutant proteins associate with wild-type PRC1, suggesting that phosphorylation of Thr470 does not alter PRC1 self-association. In addition, in vitro co-sedimentation experiment showed that PRC1 binds to microtubule independent of the phosphorylation state of Thr470. Gel-filtration experiment suggested that phosphorylation of Thr470 promotes oligomerization of PRC1. Given the fact that prevention of the Thr470 phosphorylation inhibits PRC1 oligomerization in vitro and causes an aberrant organization of central spindle in vivo, we propose that this phosphorylation-dependent PRC1 oligomerization ensures that central spindle assembly occurs at the appropriate time in the cell cycle. © 2007 IBCB, SIBS, CAS All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/136776
ISSN
2014 Impact Factor: 12.413
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFu, Cen_HK
dc.contributor.authorYan, Fen_HK
dc.contributor.authorWu, Fen_HK
dc.contributor.authorWu, Qen_HK
dc.contributor.authorWhittaker, Jen_HK
dc.contributor.authorHu, Hen_HK
dc.contributor.authorHu, Ren_HK
dc.contributor.authorYao, Xen_HK
dc.date.accessioned2011-07-29T02:12:02Z-
dc.date.available2011-07-29T02:12:02Z-
dc.date.issued2007en_HK
dc.identifier.citationCell Research, 2007, v. 17 n. 5, p. 449-457en_HK
dc.identifier.issn1001-0602en_HK
dc.identifier.urihttp://hdl.handle.net/10722/136776-
dc.description.abstractDuring cell division, chromosome segregation is orchestrated by the interaction of spindle microtubules with the centromere. A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis. Central spindle organization requires mitotic kinesins, the chromosomal passenger protein complex, and microtubule bundling protein PRC1. PRC1 is phosphorylated by Cdc2 at Thr470 and Thr481 during mitosis. However, the functional relevance of PRC1 phosphorylation at Thr470 has remained elusive. Here we show that expression of the non-phosphorylatable mutant PRC1 T470A but not the phospho-mimicking mutant PRC1 T470E causes aberrant organization of the central spindle. Immunoprecipitation experiment indicates that both PRC1 T470A and PRC1 T470E mutant proteins associate with wild-type PRC1, suggesting that phosphorylation of Thr470 does not alter PRC1 self-association. In addition, in vitro co-sedimentation experiment showed that PRC1 binds to microtubule independent of the phosphorylation state of Thr470. Gel-filtration experiment suggested that phosphorylation of Thr470 promotes oligomerization of PRC1. Given the fact that prevention of the Thr470 phosphorylation inhibits PRC1 oligomerization in vitro and causes an aberrant organization of central spindle in vivo, we propose that this phosphorylation-dependent PRC1 oligomerization ensures that central spindle assembly occurs at the appropriate time in the cell cycle. © 2007 IBCB, SIBS, CAS All rights reserved.en_HK
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.htmlen_HK
dc.relation.ispartofCell Researchen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshCell Cycle Proteins - metabolismen_HK
dc.subject.meshHeLa Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMicrotubules - metabolism - ultrastructureen_HK
dc.subject.meshMitotic Spindle Apparatus - drug effects - physiologyen_HK
dc.subject.meshPhosphorylationen_HK
dc.subject.meshProtein Structure, Quaternaryen_HK
dc.subject.meshThreonine - metabolismen_HK
dc.titleMitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organizationen_HK
dc.typeArticleen_HK
dc.identifier.emailFu, C:chuanhai@hku.hken_HK
dc.identifier.authorityFu, C=rp01515en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/cr.2007.32en_HK
dc.identifier.pmid17438553en_HK
dc.identifier.scopuseid_2-s2.0-34248594807en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34248594807&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue5en_HK
dc.identifier.spage449en_HK
dc.identifier.epage457en_HK
dc.identifier.eissn1748-7838-
dc.identifier.isiWOS:000247525700009-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridFu, C=8583808400en_HK
dc.identifier.scopusauthoridYan, F=35745269200en_HK
dc.identifier.scopusauthoridWu, F=7403465447en_HK
dc.identifier.scopusauthoridWu, Q=24451485000en_HK
dc.identifier.scopusauthoridWhittaker, J=36921005600en_HK
dc.identifier.scopusauthoridHu, H=24764424600en_HK
dc.identifier.scopusauthoridHu, R=7202640826en_HK
dc.identifier.scopusauthoridYao, X=7402530401en_HK

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