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A Dual Inhibitory Mechanism Sufficient to Maintain Cell-Cycle-Restricted CENP-A Assembly

2017-01-19Journal article Open access
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dc.contributor.authorStankovic, Ana
dc.contributor.authorGuo, Lucie Y.
dc.contributor.authorMata, João F.
dc.contributor.authorBodor, Dani L.
dc.contributor.authorCao, Xing-Jun
dc.contributor.authorBailey, Aaron O.
dc.contributor.authorShabanowitz, Jeffrey
dc.contributor.authorHunt, Donald F.
dc.contributor.authorGarcia, Benjamin A.
dc.contributor.authorBlack, Ben E.
dc.contributor.authorJansen, Lars E.T.
dc.date.accessioned2017-11-13T12:59:58Z
dc.date.available2018-01-19T01:30:09Z
dc.date.issued2017-01-19
dc.descriptionThe deposited article is a post-print version and has peer review. The deposited article version contains attached the supplementary materials within the pdf. This publication hasn't any creative commons license associated.pt_PT
dc.description.abstractChromatin featuring the H3 variant CENP-A at the centromere is critical for its mitotic function and epigenetic maintenance. Assembly of centromeric chromatin is restricted to G1 phase through inhibitory action of Cdk1/2 kinases in other phases of the cell cycle. Here, we identify the two key targets sufficient to maintain cell-cycle control of CENP-A assembly. We uncovered a single phosphorylation site in the licensing factor M18BP1 and a cyclin A binding site in the CENP-A chaperone, HJURP, that mediated specific inhibitory phosphorylation. Simultaneous expression of mutant proteins lacking these residues results in complete uncoupling from the cell cycle. Consequently, CENP-A assembly is fully recapitulated under high Cdk activities, indistinguishable from G1 assembly. We find that Cdk-mediated inhibition is exerted by sequestering active factors away from the centromere. Finally, we show that displacement of M18BP1 from the centromere is critical for the assembly mechanism of CENP-A.pt_PT
dc.description.sponsorshipFundação para a Ciência e a Tecnologia grants: (SFRH/BD/51878/2012, SFRH/BD/74284/2010, BIA-BCM/100557/2008); NIH/National Institute of General Medical Sciences grants: (R01-GM082989; T32-GM008275); NIH/NCI grant: (F30-CA186430); NIH grants (GM 037537, GM 110174); EMBO installation grant: (1818); ERC-consolidator grant: (ERC-2013-CoG-615638).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationAna Stankovic, Lucie Y. Guo, João F. Mata, Dani L. Bodor, Xing-Jun Cao, Aaron O. Bailey, Jeffrey Shabanowitz, Donald F. Hunt, Benjamin A. Garcia, Ben E. Black, Lars E.T. Jansen, A Dual Inhibitory Mechanism Sufficient to Maintain Cell-Cycle-Restricted CENP-A Assembly, In Molecular Cell, Volume 65, Issue 2, 2017, Pages 231-246, ISSN 1097-2765, https://doi.org/10.1016/j.molcel.2016.11.021. (http://www.sciencedirect.com/science/article/pii/S1097276516307572)pt_PT
dc.identifier.doi10.1016/j.molcel.2016.11.021pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/804
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationR01-GM082989pt_PT
dc.relationEPIGENETIC AND CELL CYCLE CONTROL OF CENTROMERE INHERITANCE
dc.relationF30-CA186430pt_PT
dc.relationGM 037537pt_PT
dc.relationGM 110174pt_PT
dc.relationEMBO installation grant 1818pt_PT
dc.relationMechanisms of Chromatin-based Epigenetic Inheritance
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S1097276516307572?via%3Dihubpt_PT
dc.subjectcentromerept_PT
dc.subjecthistone variantpt_PT
dc.subjectCENP-Apt_PT
dc.subjectmitosispt_PT
dc.subjectepigeneticspt_PT
dc.subjectchromatinpt_PT
dc.subjectcyclin dependent kinasept_PT
dc.subjectcell cyclept_PT
dc.subjectkinetochorept_PT
dc.titleA Dual Inhibitory Mechanism Sufficient to Maintain Cell-Cycle-Restricted CENP-A Assemblypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleEPIGENETIC AND CELL CYCLE CONTROL OF CENTROMERE INHERITANCE
oaire.awardTitleMechanisms of Chromatin-based Epigenetic Inheritance
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F51878%2F2012/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F74284%2F2010/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-BCM%2F100557%2F2008/PT
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/615638/EU
oaire.citation.endPage246pt_PT
oaire.citation.issue2pt_PT
oaire.citation.startPage231pt_PT
oaire.citation.titleMolecular Cellpt_PT
oaire.citation.volume65pt_PT
oaire.fundingStreamSFRH
oaire.fundingStream3599-PPCDT
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameEuropean Commission
rcaap.embargofctThe deposited article has 12 months of embargo period in terms of access, because of the journal's policies and the publisher's copyright policy, which require a period of embargo of 12 months.pt_PT
rcaap.rightsembargoedAccesspt_PT
rcaap.typearticlept_PT
relation.isProjectOfPublicationf37ae656-1401-424a-9f2e-a6f1d6ad2a39
relation.isProjectOfPublication74531c77-3c24-405b-9787-ccb627a42ee8
relation.isProjectOfPublication920402dc-3fe1-4134-b1c7-1e51333ae32f
relation.isProjectOfPublicationfc0420ff-72cc-4e0d-8521-76c288c7a6a5
relation.isProjectOfPublication.latestForDiscovery920402dc-3fe1-4134-b1c7-1e51333ae32f

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