Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments

Detalhes bibliográficos
Autor(a) principal: Silva, Patricia M. A.
Data de Publicação: 2015
Outros Autores: Tavares, Alvaro A., 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/10400.1/11770
Resumo: We previously reported that the spindle assembly checkpoint protein Bub3 is involved in regulating kinetochore-microtubule (KT-MT) attachments. Also, Bub3 was reported to interact with the microtubule motor protein dynein. Here we examined how this interaction contributes to KT-MT attachments. Depletion of Bub3 or dynein induced misaligned chromosomes, consistent with their role in KT-MT attachments. Unexpectedly, co-silencing of both proteins partially suppressed the misalignment phenotype and restored chromosome congression. Consistent with these observations, KT-MT attachments in co-depleted cells were stable, able to drive chromosome congression, and produce inter-and intra-kinetochore stretch, indicating they are functional. We suggest that a mutual antagonism exists between Bub3 and dynein to ensure optimal KT-MT attachments. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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spelling Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachmentsSpindle-assembly checkpointCytoplasmic dyneinMitotic checkpointMitosisCongressionProteinCellsWe previously reported that the spindle assembly checkpoint protein Bub3 is involved in regulating kinetochore-microtubule (KT-MT) attachments. Also, Bub3 was reported to interact with the microtubule motor protein dynein. Here we examined how this interaction contributes to KT-MT attachments. Depletion of Bub3 or dynein induced misaligned chromosomes, consistent with their role in KT-MT attachments. Unexpectedly, co-silencing of both proteins partially suppressed the misalignment phenotype and restored chromosome congression. Consistent with these observations, KT-MT attachments in co-depleted cells were stable, able to drive chromosome congression, and produce inter-and intra-kinetochore stretch, indicating they are functional. We suggest that a mutual antagonism exists between Bub3 and dynein to ensure optimal KT-MT attachments. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.CESPU [02-GCQF-CICS-2011N]; FCT - Fundacao para a Ciencia e a Tecnologia [CEQUIMED-PEst-OE/SAU/UI4040/2014]; FCT [SFRH/BD/90744/2012]Elsevier Science BvSapientiaSilva, Patricia M. A.Tavares, Alvaro A.Bousbaa, Hassan2018-12-07T14:57:55Z2015-112015-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11770eng0014-579310.1016/j.febslet.2015.10.017info: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:RCAAP2023-07-24T10:23:37Zoai:sapientia.ualg.pt:10400.1/11770Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:03:13.718990Repositório 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 Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
title Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
spellingShingle Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
Silva, Patricia M. A.
Spindle-assembly checkpoint
Cytoplasmic dynein
Mitotic checkpoint
Mitosis
Congression
Protein
Cells
title_short Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
title_full Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
title_fullStr Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
title_full_unstemmed Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
title_sort Co-silencing of human Bub3 and dynein highlights an antagonistic relationship in regulating kinetochore-microtubule attachments
author Silva, Patricia M. A.
author_facet Silva, Patricia M. A.
Tavares, Alvaro A.
Bousbaa, Hassan
author_role author
author2 Tavares, Alvaro A.
Bousbaa, Hassan
author2_role author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv Silva, Patricia M. A.
Tavares, Alvaro A.
Bousbaa, Hassan
dc.subject.por.fl_str_mv Spindle-assembly checkpoint
Cytoplasmic dynein
Mitotic checkpoint
Mitosis
Congression
Protein
Cells
topic Spindle-assembly checkpoint
Cytoplasmic dynein
Mitotic checkpoint
Mitosis
Congression
Protein
Cells
description We previously reported that the spindle assembly checkpoint protein Bub3 is involved in regulating kinetochore-microtubule (KT-MT) attachments. Also, Bub3 was reported to interact with the microtubule motor protein dynein. Here we examined how this interaction contributes to KT-MT attachments. Depletion of Bub3 or dynein induced misaligned chromosomes, consistent with their role in KT-MT attachments. Unexpectedly, co-silencing of both proteins partially suppressed the misalignment phenotype and restored chromosome congression. Consistent with these observations, KT-MT attachments in co-depleted cells were stable, able to drive chromosome congression, and produce inter-and intra-kinetochore stretch, indicating they are functional. We suggest that a mutual antagonism exists between Bub3 and dynein to ensure optimal KT-MT attachments. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
publishDate 2015
dc.date.none.fl_str_mv 2015-11
2015-11-01T00:00:00Z
2018-12-07T14:57:55Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.1/11770
url http://hdl.handle.net/10400.1/11770
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0014-5793
10.1016/j.febslet.2015.10.017
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publisher.none.fl_str_mv Elsevier Science Bv
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