Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/127043
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dc.creatorMangal, S-
dc.creatorSacher, J-
dc.creatorKim, T-
dc.creatorOsório, DS-
dc.creatorMotegi, F-
dc.creatorCarvalho, AX-
dc.creatorOegema, K-
dc.creatorZanin, E-
dc.date.accessioned2020-05-13T10:50:29Z-
dc.date.available2020-05-13T10:50:29Z-
dc.date.issued2018-
dc.identifier.issn0021-9525-
dc.identifier.urihttps://hdl.handle.net/10216/127043-
dc.description.abstractDuring cytokinesis, a signal from the central spindle that forms between the separating anaphase chromosomes promotes the accumulation of contractile ring components at the cell equator, while a signal from the centrosomal microtubule asters inhibits accumulation of contractile ring components at the cell poles. However, the molecular identity of the inhibitory signal has remained unknown. To identify molecular components of the aster-based inhibitory signal, we developed a means to monitor the removal of contractile ring proteins from the polar cortex after anaphase onset. Using this assay, we show that polar clearing is an active process that requires activation of Aurora A kinase by TPXL-1. TPXL-1 concentrates on astral microtubules coincident with polar clearing in anaphase, and its ability to recruit Aurora A and activate its kinase activity are essential for clearing. In summary, our data identify Aurora A kinase as an aster-based inhibitory signal that restricts contractile ring components to the cell equator during cytokinesis.-
dc.description.sponsorshipWe thank the Caenorhabditis Genetic Center (funded by the National Institutes of Health Office of Research Infrastructure Programs P40 OD010440) for strains. This work was supported by grants to K. Oegema (National Institutes of Health; GM074207), E. Zanin (Deutsche Forschungsgemeinschaft, ZA619/3-1), and A.X. Carvalho (European Research Council; 640553–ACTOMYO). T. Kim was supported by a grant to Arshad Desai (National Institutes of Health; GM074215). K. Oegema receives salary and other support from the Ludwig Institute for Cancer Research. S. Mangal is a member of International Max Planck Research School for Molecular Life Sciences, and J. Sacher is a member of the Life Science Munich graduate program; both thank their programs for support.-
dc.language.isoeng-
dc.publisherRockefeller University Press-
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/640553/EU-
dc.relation.ispartofJournal of Cell Biology, vol.217(3), p. 837-848-
dc.rightsopenAccess-
dc.rights.urihttps ://creativecommons.org/licenses/by-nc-sa/4.0/-
dc.subject.meshAnaphase / physiology-
dc.subject.meshAnimals-
dc.subject.meshAurora Kinase A / genetics-
dc.subject.meshAurora Kinase A / metabolismo-
dc.subject.meshCaenorhabditis elegans / genetics-
dc.subject.meshCaenorhabditis elegans / metabolismo-
dc.subject.meshCaenorhabditis elegans Proteins / genetics-
dc.subject.meshCaenorhabditis elegans Proteins / metabolismo-
dc.subject.meshCarrier Proteins / genetics-
dc.subject.meshCarrier Proteins / metabolismo-
dc.subject.meshCytokinesis / physiology-
dc.subject.meshEnzyme Activation / physiology-
dc.subject.meshMicrotubules / genetics-
dc.subject.meshMicrotubules / metabolismo-
dc.subject.meshSignal Transduction / physiology-
dc.titleTPXL-1 activates Aurora A to clear contractile ring components from the polar cortex during cytokinesis-
dc.typeArtigo em Revista Científica Internacional-
dc.contributor.uportoInstituto de Investigação e Inovação em Saúde-
dc.identifier.doi10.1083/jcb.201706021-
dc.relation.publisherversionhttps://rupress.org/jcb/article-lookup/doi/10.1083/jcb.201706021-
Appears in Collections:I3S - Artigo em Revista Científica Internacional

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