Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation

Detalhes bibliográficos
Autor(a) principal: Lemos, CL
Data de Publicação: 2000
Outros Autores: Sampaio, P, Maiato, H, Costa, M, Omel’yanchuk, LV, Liberal, V, Sunkel, CE
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10216/53559
Resumo: Through mutational analysis in Drosophila, we have identified the gene multiple asters (mast), that encodes a new 165 kDa protein. mast mutant neuroblasts are highly polyploid and show severe mitotic abnormalities including the formation of mono- and multi-polar spindles organised by an irregular number of MTOCs of abnormal size and shape. The mast gene product is evolutionary conserved since homologues were identified from yeast to man, revealing a novel protein family. Antibodies against Mast and analysis of tissue culture cells expressing an EGFP-Mast fusion protein show that during mitosis this protein localises to centrosomes, the mitotic spindle, centromeres and spindle midzone. Microtubule-binding assays indicate that Mast is a microtubule-associated protein displaying strong affinity for polymerised microtubules. The defects observed in the mutant alleles and the intracellular localisation of the protein suggest that Mast plays an essential role in centrosome separation and organisation of the bipolar mitotic spindle.
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spelling Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisationCentrosomeDrosophilaMAPsMicrotubulesMitosisThrough mutational analysis in Drosophila, we have identified the gene multiple asters (mast), that encodes a new 165 kDa protein. mast mutant neuroblasts are highly polyploid and show severe mitotic abnormalities including the formation of mono- and multi-polar spindles organised by an irregular number of MTOCs of abnormal size and shape. The mast gene product is evolutionary conserved since homologues were identified from yeast to man, revealing a novel protein family. Antibodies against Mast and analysis of tissue culture cells expressing an EGFP-Mast fusion protein show that during mitosis this protein localises to centrosomes, the mitotic spindle, centromeres and spindle midzone. Microtubule-binding assays indicate that Mast is a microtubule-associated protein displaying strong affinity for polymerised microtubules. The defects observed in the mutant alleles and the intracellular localisation of the protein suggest that Mast plays an essential role in centrosome separation and organisation of the bipolar mitotic spindle.20002000-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10216/53559eng0261-4189Lemos, CLSampaio, PMaiato, HCosta, MOmel’yanchuk, LVLiberal, VSunkel, CEinfo: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:RCAAP2023-11-29T14:36:02Zoai:repositorio-aberto.up.pt:10216/53559Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:04:52.052957Repositório 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 Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
title Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
spellingShingle Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
Lemos, CL
Centrosome
Drosophila
MAPs
Microtubules
Mitosis
title_short Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
title_full Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
title_fullStr Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
title_full_unstemmed Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
title_sort Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
author Lemos, CL
author_facet Lemos, CL
Sampaio, P
Maiato, H
Costa, M
Omel’yanchuk, LV
Liberal, V
Sunkel, CE
author_role author
author2 Sampaio, P
Maiato, H
Costa, M
Omel’yanchuk, LV
Liberal, V
Sunkel, CE
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Lemos, CL
Sampaio, P
Maiato, H
Costa, M
Omel’yanchuk, LV
Liberal, V
Sunkel, CE
dc.subject.por.fl_str_mv Centrosome
Drosophila
MAPs
Microtubules
Mitosis
topic Centrosome
Drosophila
MAPs
Microtubules
Mitosis
description Through mutational analysis in Drosophila, we have identified the gene multiple asters (mast), that encodes a new 165 kDa protein. mast mutant neuroblasts are highly polyploid and show severe mitotic abnormalities including the formation of mono- and multi-polar spindles organised by an irregular number of MTOCs of abnormal size and shape. The mast gene product is evolutionary conserved since homologues were identified from yeast to man, revealing a novel protein family. Antibodies against Mast and analysis of tissue culture cells expressing an EGFP-Mast fusion protein show that during mitosis this protein localises to centrosomes, the mitotic spindle, centromeres and spindle midzone. Microtubule-binding assays indicate that Mast is a microtubule-associated protein displaying strong affinity for polymerised microtubules. The defects observed in the mutant alleles and the intracellular localisation of the protein suggest that Mast plays an essential role in centrosome separation and organisation of the bipolar mitotic spindle.
publishDate 2000
dc.date.none.fl_str_mv 2000
2000-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10216/53559
url http://hdl.handle.net/10216/53559
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0261-4189
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dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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