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Article: Dynamic Autophosphorylation of Mps1 Kinase Is Required for Faithful Mitotic Progression

TitleDynamic Autophosphorylation of Mps1 Kinase Is Required for Faithful Mitotic Progression
Authors
Issue Date2014
Citation
PLoS ONE, 2014, v. 9 n. 9, p. e104723 How to Cite?
AbstractThe spindle assembly checkpoint (SAC) is a surveillance mechanism monitoring cell cycle progression, thus ensuring accurate chromosome segregation. The conserved mitotic kinase Mps1 is a key component of the SAC. The human Mps1 exhibits comprehensive phosphorylation during mitosis. However, the related biological relevance is largely unknown. Here, we demonstrate that 8 autophosphorylation sites within the N-terminus of Mps1, outside of the catalytic domain, are involved in regulating Mps1 kinetochore localization. The phospho-mimicking mutant of the 8 autophosphorylation sites impairs Mps1 localization to kinetochore and also affects the kinetochore recruitment of BubR1 and Mad2, two key SAC effectors, subsequently leading to chromosome segregation errors. Interestingly, the non-phosphorylatable mutant of the 8 autophosphorylation sites enhances Mps1 kinetochore localization and delays anaphase onset. We further show that the Mps1 phospho-mimicking and non-phosphorylatable mutants do not affect metaphase chromosome congression. Thus, our results highlight the importance of dynamic autophosphorylation of Mps1 in regulating accurate chromosome segregation and ensuring proper mitotic progression.
Persistent Identifierhttp://hdl.handle.net/10722/207223
ISSN
2015 Impact Factor: 3.057
2015 SCImago Journal Rankings: 1.395
ISI Accession Number ID
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DC FieldValueLanguage
dc.contributor.authorWang, Xen_US
dc.contributor.authorYu, Hen_US
dc.contributor.authorXu, Len_US
dc.contributor.authorZhu, Ten_US
dc.contributor.authorZHENG, Fen_US
dc.contributor.authorFu, Cen_US
dc.contributor.authorWang, Zen_US
dc.contributor.authorDou, Zen_US
dc.date.accessioned2014-12-19T09:00:44Z-
dc.date.available2014-12-19T09:00:44Z-
dc.date.issued2014en_US
dc.identifier.citationPLoS ONE, 2014, v. 9 n. 9, p. e104723en_US
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/10722/207223-
dc.description.abstractThe spindle assembly checkpoint (SAC) is a surveillance mechanism monitoring cell cycle progression, thus ensuring accurate chromosome segregation. The conserved mitotic kinase Mps1 is a key component of the SAC. The human Mps1 exhibits comprehensive phosphorylation during mitosis. However, the related biological relevance is largely unknown. Here, we demonstrate that 8 autophosphorylation sites within the N-terminus of Mps1, outside of the catalytic domain, are involved in regulating Mps1 kinetochore localization. The phospho-mimicking mutant of the 8 autophosphorylation sites impairs Mps1 localization to kinetochore and also affects the kinetochore recruitment of BubR1 and Mad2, two key SAC effectors, subsequently leading to chromosome segregation errors. Interestingly, the non-phosphorylatable mutant of the 8 autophosphorylation sites enhances Mps1 kinetochore localization and delays anaphase onset. We further show that the Mps1 phospho-mimicking and non-phosphorylatable mutants do not affect metaphase chromosome congression. Thus, our results highlight the importance of dynamic autophosphorylation of Mps1 in regulating accurate chromosome segregation and ensuring proper mitotic progression.-
dc.languageengen_US
dc.relation.ispartofPLoS ONEen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleDynamic Autophosphorylation of Mps1 Kinase Is Required for Faithful Mitotic Progressionen_US
dc.typeArticleen_US
dc.identifier.emailFu, C: chuanhai@hku.hken_US
dc.identifier.authorityFu, C=rp01515en_US
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.pone.0104723en_US
dc.identifier.pmid25265012-
dc.identifier.hkuros241975en_US
dc.identifier.volume9en_US
dc.identifier.spagee104723en_US
dc.identifier.epagee104723en_US
dc.identifier.isiWOS:000345745400002-
dc.relation.projectMolecular mechanisms regulating the interactions between mitochondria and the microtubule cytoskeleton-
dc.relation.projectSystematic investigation of the roles of mitotic kinesins in spindle dynamics-

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