Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin.
Autor(a) principal: | |
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Data de Publicação: | 2011 |
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/1822/15397 |
Resumo: | The Karyopherin (Kap) family of nuclear transport receptors enables trafficking of proteins to and from the nucleus in a precise, regulated manner. Individual members function in overlapping pathways, while simultaneously being very specific for their main cargoes. The details of this apparent contradiction and rules governing pathway preference remain to be further elucidated. S. cerevisiae Lhp1 is an abundant protein that functions as an RNA chaperone in a variety of biologically important processes. It localizes almost exclusively to the nucleus and is imported by Kap108. We show that mutation of 3 of the 275 residues in Lhp1 alters its import pathway to a Kap121-dependent process. This mutant does not retain wild-type function and is bound by several chaperones. We propose that Kap121 also acts as a chaperone, one that can act as a genetic buffer by transporting mutated proteins to the nucleus. |
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spelling |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin.Nuclear transportYeastScience & TechnologyThe Karyopherin (Kap) family of nuclear transport receptors enables trafficking of proteins to and from the nucleus in a precise, regulated manner. Individual members function in overlapping pathways, while simultaneously being very specific for their main cargoes. The details of this apparent contradiction and rules governing pathway preference remain to be further elucidated. S. cerevisiae Lhp1 is an abundant protein that functions as an RNA chaperone in a variety of biologically important processes. It localizes almost exclusively to the nucleus and is imported by Kap108. We show that mutation of 3 of the 275 residues in Lhp1 alters its import pathway to a Kap121-dependent process. This mutant does not retain wild-type function and is bound by several chaperones. We propose that Kap121 also acts as a chaperone, one that can act as a genetic buffer by transporting mutated proteins to the nucleus.Fundação para a Ciência e a Tecnologia (FCT)Public Library of ScienceUniversidade do MinhoChaves, S. R.Rosenblum, Jonathan S.2011-02-092011-02-09T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/15397eng1932-620310.1371/journal.pone.001684621347375http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0016846info: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:RCAAP2023-07-21T12:34:27Zoai:repositorium.sdum.uminho.pt:1822/15397Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:30:09.195492Repositório 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 |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
title |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
spellingShingle |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. Chaves, S. R. Nuclear transport Yeast Science & Technology |
title_short |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
title_full |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
title_fullStr |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
title_full_unstemmed |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
title_sort |
Efficient nuclear transport of structurally disturbed cargo: mutations in a cargo protein switch its cognate karyopherin. |
author |
Chaves, S. R. |
author_facet |
Chaves, S. R. Rosenblum, Jonathan S. |
author_role |
author |
author2 |
Rosenblum, Jonathan S. |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Chaves, S. R. Rosenblum, Jonathan S. |
dc.subject.por.fl_str_mv |
Nuclear transport Yeast Science & Technology |
topic |
Nuclear transport Yeast Science & Technology |
description |
The Karyopherin (Kap) family of nuclear transport receptors enables trafficking of proteins to and from the nucleus in a precise, regulated manner. Individual members function in overlapping pathways, while simultaneously being very specific for their main cargoes. The details of this apparent contradiction and rules governing pathway preference remain to be further elucidated. S. cerevisiae Lhp1 is an abundant protein that functions as an RNA chaperone in a variety of biologically important processes. It localizes almost exclusively to the nucleus and is imported by Kap108. We show that mutation of 3 of the 275 residues in Lhp1 alters its import pathway to a Kap121-dependent process. This mutant does not retain wild-type function and is bound by several chaperones. We propose that Kap121 also acts as a chaperone, one that can act as a genetic buffer by transporting mutated proteins to the nucleus. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-02-09 2011-02-09T00:00:00Z |
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/1822/15397 |
url |
http://hdl.handle.net/1822/15397 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1932-6203 10.1371/journal.pone.0016846 21347375 http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0016846 |
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.publisher.none.fl_str_mv |
Public Library of Science |
publisher.none.fl_str_mv |
Public Library of Science |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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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1799132803767468032 |