Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organisation
Autor(a) principal: | |
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Data de Publicação: | 2000 |
Outros Autores: | , , , , , |
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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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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 |
format |
article |
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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
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 instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
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 |
repository.mail.fl_str_mv |
|
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1799135972745543681 |