Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis

Detalhes bibliográficos
Autor(a) principal: Ferreira, João Vasco
Data de Publicação: 2019
Outros Autores: Soares, Ana Rosa, Ramalho, José S., Ribeiro-Rodrigues, Teresa, Máximo, Catarina, Zuzarte, Mónica, Girão, Henrique, Pereira, Paulo
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/107237
https://doi.org/10.1371/journal.pone.0223790
Resumo: Deregulation of proteostasis is a main feature of many age-related diseases, often leading to the accumulation of toxic oligomers and insoluble protein aggregates that accumulate intracellularly or in the extracellular space. To understand the mechanisms whereby toxic or otherwise unwanted proteins are secreted to the extracellular space, we inactivated the quality-control and proteostasis regulator ubiquitin ligase STUB1/CHIP. Data indicated that STUB1 deficiency leads both to the intracellular accumulation of protein aggregates and to an increase in the secretion of small extracellular vesicles (sEVs), including exosomes. Secreted sEVs are enriched in ubiquitinated and/or undegraded proteins and protein oligomers. Data also indicates that oxidative stress induces an increase in the release of sEVs in cells depleted from STUB1. Overall, the results presented here suggest that cells use exosomes to dispose of damaged and/or undegraded proteins as a means to reduce intracellular accumulation of proteotoxic material.
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spelling Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasisDeregulation of proteostasis is a main feature of many age-related diseases, often leading to the accumulation of toxic oligomers and insoluble protein aggregates that accumulate intracellularly or in the extracellular space. To understand the mechanisms whereby toxic or otherwise unwanted proteins are secreted to the extracellular space, we inactivated the quality-control and proteostasis regulator ubiquitin ligase STUB1/CHIP. Data indicated that STUB1 deficiency leads both to the intracellular accumulation of protein aggregates and to an increase in the secretion of small extracellular vesicles (sEVs), including exosomes. Secreted sEVs are enriched in ubiquitinated and/or undegraded proteins and protein oligomers. Data also indicates that oxidative stress induces an increase in the release of sEVs in cells depleted from STUB1. Overall, the results presented here suggest that cells use exosomes to dispose of damaged and/or undegraded proteins as a means to reduce intracellular accumulation of proteotoxic material.Public Library of Science2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/107237http://hdl.handle.net/10316/107237https://doi.org/10.1371/journal.pone.0223790eng1932-6203316139221932-6203Ferreira, João VascoSoares, Ana RosaRamalho, José S.Ribeiro-Rodrigues, TeresaMáximo, CatarinaZuzarte, MónicaGirão, HenriquePereira, Pauloinfo: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:RCAAP2023-06-15T11:28:12Zoai:estudogeral.uc.pt:10316/107237Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:23:37.547230Repositório 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 Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
title Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
spellingShingle Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
Ferreira, João Vasco
title_short Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
title_full Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
title_fullStr Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
title_full_unstemmed Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
title_sort Exosomes and STUB1/CHIP cooperate to maintain intracellular proteostasis
author Ferreira, João Vasco
author_facet Ferreira, João Vasco
Soares, Ana Rosa
Ramalho, José S.
Ribeiro-Rodrigues, Teresa
Máximo, Catarina
Zuzarte, Mónica
Girão, Henrique
Pereira, Paulo
author_role author
author2 Soares, Ana Rosa
Ramalho, José S.
Ribeiro-Rodrigues, Teresa
Máximo, Catarina
Zuzarte, Mónica
Girão, Henrique
Pereira, Paulo
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Ferreira, João Vasco
Soares, Ana Rosa
Ramalho, José S.
Ribeiro-Rodrigues, Teresa
Máximo, Catarina
Zuzarte, Mónica
Girão, Henrique
Pereira, Paulo
description Deregulation of proteostasis is a main feature of many age-related diseases, often leading to the accumulation of toxic oligomers and insoluble protein aggregates that accumulate intracellularly or in the extracellular space. To understand the mechanisms whereby toxic or otherwise unwanted proteins are secreted to the extracellular space, we inactivated the quality-control and proteostasis regulator ubiquitin ligase STUB1/CHIP. Data indicated that STUB1 deficiency leads both to the intracellular accumulation of protein aggregates and to an increase in the secretion of small extracellular vesicles (sEVs), including exosomes. Secreted sEVs are enriched in ubiquitinated and/or undegraded proteins and protein oligomers. Data also indicates that oxidative stress induces an increase in the release of sEVs in cells depleted from STUB1. Overall, the results presented here suggest that cells use exosomes to dispose of damaged and/or undegraded proteins as a means to reduce intracellular accumulation of proteotoxic material.
publishDate 2019
dc.date.none.fl_str_mv 2019
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10316/107237
http://hdl.handle.net/10316/107237
https://doi.org/10.1371/journal.pone.0223790
url http://hdl.handle.net/10316/107237
https://doi.org/10.1371/journal.pone.0223790
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1932-6203
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