The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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/10773/29271 |
Resumo: | Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases. |
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The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrateProtein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases.Public Library of Science2020-09-21T10:22:41Z2013-10-07T00:00:00Z2013-10-07info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/29271eng1932-620310.1371/journal.pone.0076788Santos, MarianaRebelo, SandraVan Kleeff, Paula J. M.Kim, Connie E.Dauer, William T.Fardilha, MargaridaSilva, Odete A. da Cruz eSilva, Edgar F. da Cruz einfo: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:RCAAP2024-02-22T11:56:38Zoai:ria.ua.pt:10773/29271Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:01:39.113501Repositório 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 |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
title |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
spellingShingle |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate Santos, Mariana |
title_short |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
title_full |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
title_fullStr |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
title_full_unstemmed |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
title_sort |
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate |
author |
Santos, Mariana |
author_facet |
Santos, Mariana Rebelo, Sandra Van Kleeff, Paula J. M. Kim, Connie E. Dauer, William T. Fardilha, Margarida Silva, Odete A. da Cruz e Silva, Edgar F. da Cruz e |
author_role |
author |
author2 |
Rebelo, Sandra Van Kleeff, Paula J. M. Kim, Connie E. Dauer, William T. Fardilha, Margarida Silva, Odete A. da Cruz e Silva, Edgar F. da Cruz e |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Santos, Mariana Rebelo, Sandra Van Kleeff, Paula J. M. Kim, Connie E. Dauer, William T. Fardilha, Margarida Silva, Odete A. da Cruz e Silva, Edgar F. da Cruz e |
description |
Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-10-07T00:00:00Z 2013-10-07 2020-09-21T10:22:41Z |
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/10773/29271 |
url |
http://hdl.handle.net/10773/29271 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1932-6203 10.1371/journal.pone.0076788 |
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 |
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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) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137672527085568 |