Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles

Detalhes bibliográficos
Autor(a) principal: Silva, PMA; Patrícia M.A. Silva
Data de Publicação: 2014
Outros Autores: Reis, Rita M., Bolanos-Garcia, Victor M., Florindo, Claudia, Tavares, Alvaro, Bousbaa, Hassan
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.1/11191
Resumo: A predominant mechanism of spindle assembly checkpoint (SAC) silencing is dynein-mediated transport of certain kinetochore proteins along microtubules. There are still conflicting data as to which SAC proteins are dynein cargoes. Using two ATP reduction assays, we found that the core SAC proteins Mad1, Mad2, Bub1, BubR1, and Bub3 redistributed from attached kinetochores to spindle poles, in a dynein-dependent manner. This redistribution still occurred in metaphase-arrested cells, at a time when the SAC should be satisfied and silenced. Unexpectedly, we found that a pool of Hec1 and Mis12 also relocalizes to spindle poles, suggesting KMN components as additional dynein cargoes. The potential significance of these results for SAC silencing is discussed. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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spelling Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle polesMitotic checkpointMicrotubule attachmentChromosome alignmentBub3 stabilityLiving cellsComplexApc/cInhibitionCdc20Hec1A predominant mechanism of spindle assembly checkpoint (SAC) silencing is dynein-mediated transport of certain kinetochore proteins along microtubules. There are still conflicting data as to which SAC proteins are dynein cargoes. Using two ATP reduction assays, we found that the core SAC proteins Mad1, Mad2, Bub1, BubR1, and Bub3 redistributed from attached kinetochores to spindle poles, in a dynein-dependent manner. This redistribution still occurred in metaphase-arrested cells, at a time when the SAC should be satisfied and silenced. Unexpectedly, we found that a pool of Hec1 and Mis12 also relocalizes to spindle poles, suggesting KMN components as additional dynein cargoes. The potential significance of these results for SAC silencing is discussed. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.CESPU [02-GCQF-CICS-2011N]; national Portuguese funding through FCT - Fundacao para a Ciencia e a Tecnologia FCT [POCTI/BIA/PRO/60337/2004, PTDC/SAU-OBD/105234/2008]; FCT [PEst-OE/ EQB/LA0023/2013, SFRH/BD/90744/2012]; [EXPL/BEX-BCM/1104/2013]ElsevierSapientiaSilva, PMA; Patrícia M.A. SilvaReis, Rita M.Bolanos-Garcia, Victor M.Florindo, ClaudiaTavares, AlvaroBousbaa, Hassan2018-12-07T14:52:45Z2014-082014-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11191eng0014-5793https://doi.org/10.1016/j.febslet.2014.07.011info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:22:57Zoai:sapientia.ualg.pt:10400.1/11191Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:02:42.136271Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
title Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
spellingShingle Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
Silva, PMA; Patrícia M.A. Silva
Mitotic checkpoint
Microtubule attachment
Chromosome alignment
Bub3 stability
Living cells
Complex
Apc/c
Inhibition
Cdc20
Hec1
title_short Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
title_full Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
title_fullStr Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
title_full_unstemmed Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
title_sort Dynein-dependent transport of spindle assembly checkpoint proteins off kinetochores toward spindle poles
author Silva, PMA; Patrícia M.A. Silva
author_facet Silva, PMA; Patrícia M.A. Silva
Reis, Rita M.
Bolanos-Garcia, Victor M.
Florindo, Claudia
Tavares, Alvaro
Bousbaa, Hassan
author_role author
author2 Reis, Rita M.
Bolanos-Garcia, Victor M.
Florindo, Claudia
Tavares, Alvaro
Bousbaa, Hassan
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Silva, PMA; Patrícia M.A. Silva
Reis, Rita M.
Bolanos-Garcia, Victor M.
Florindo, Claudia
Tavares, Alvaro
Bousbaa, Hassan
dc.subject.por.fl_str_mv Mitotic checkpoint
Microtubule attachment
Chromosome alignment
Bub3 stability
Living cells
Complex
Apc/c
Inhibition
Cdc20
Hec1
topic Mitotic checkpoint
Microtubule attachment
Chromosome alignment
Bub3 stability
Living cells
Complex
Apc/c
Inhibition
Cdc20
Hec1
description A predominant mechanism of spindle assembly checkpoint (SAC) silencing is dynein-mediated transport of certain kinetochore proteins along microtubules. There are still conflicting data as to which SAC proteins are dynein cargoes. Using two ATP reduction assays, we found that the core SAC proteins Mad1, Mad2, Bub1, BubR1, and Bub3 redistributed from attached kinetochores to spindle poles, in a dynein-dependent manner. This redistribution still occurred in metaphase-arrested cells, at a time when the SAC should be satisfied and silenced. Unexpectedly, we found that a pool of Hec1 and Mis12 also relocalizes to spindle poles, suggesting KMN components as additional dynein cargoes. The potential significance of these results for SAC silencing is discussed. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
publishDate 2014
dc.date.none.fl_str_mv 2014-08
2014-08-01T00:00:00Z
2018-12-07T14:52:45Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.1/11191
url http://hdl.handle.net/10400.1/11191
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0014-5793
https://doi.org/10.1016/j.febslet.2014.07.011
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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