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Article: Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization
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TitleMitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization
 
AuthorsFu, C2 1
Yan, F2
Wu, F2
Wu, Q2
Whittaker, J1
Hu, H3
Hu, R3
Yao, X2 1
 
Issue Date2007
 
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.html
 
CitationCell Research, 2007, v. 17 n. 5, p. 449-457 [How to Cite?]
DOI: http://dx.doi.org/10.1038/cr.2007.32
 
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.
 
ISSN1001-0602
2012 Impact Factor: 10.526
2012 SCImago Journal Rankings: 3.739
 
DOIhttp://dx.doi.org/10.1038/cr.2007.32
 
ISI Accession Number IDWOS:000247525700009
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorFu, C
 
dc.contributor.authorYan, F
 
dc.contributor.authorWu, F
 
dc.contributor.authorWu, Q
 
dc.contributor.authorWhittaker, J
 
dc.contributor.authorHu, H
 
dc.contributor.authorHu, R
 
dc.contributor.authorYao, X
 
dc.date.accessioned2011-07-29T02:12:02Z
 
dc.date.available2011-07-29T02:12:02Z
 
dc.date.issued2007
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationCell Research, 2007, v. 17 n. 5, p. 449-457 [How to Cite?]
DOI: http://dx.doi.org/10.1038/cr.2007.32
 
dc.identifier.doihttp://dx.doi.org/10.1038/cr.2007.32
 
dc.identifier.eissn1748-7838
 
dc.identifier.epage457
 
dc.identifier.isiWOS:000247525700009
 
dc.identifier.issn1001-0602
2012 Impact Factor: 10.526
2012 SCImago Journal Rankings: 3.739
 
dc.identifier.issue5
 
dc.identifier.pmid17438553
 
dc.identifier.scopuseid_2-s2.0-34248594807
 
dc.identifier.spage449
 
dc.identifier.urihttp://hdl.handle.net/10722/136776
 
dc.identifier.volume17
 
dc.languageeng
 
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.html
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofCell Research
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmino Acid Sequence
 
dc.subject.meshCell Cycle Proteins - metabolism
 
dc.subject.meshHeLa Cells
 
dc.subject.meshHumans
 
dc.subject.meshMicrotubules - metabolism - ultrastructure
 
dc.subject.meshMitotic Spindle Apparatus - drug effects - physiology
 
dc.subject.meshPhosphorylation
 
dc.subject.meshProtein Structure, Quaternary
 
dc.subject.meshThreonine - metabolism
 
dc.titleMitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization
 
dc.typeArticle
 
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Author Affiliations
  1. Morehouse School of Medicine
  2. University of Science and Technology of China
  3. Huashan Hospital