Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?
Autor(a) principal: | |
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Data de Publicação: | 2021 |
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/10400.1/16735 |
Resumo: | Stress granules (SGs) are membraneless cell compartments formed in response to different stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other proteins coalesce together. SGs assembly is crucial for cell survival, since SGs are implicated in the regulation of translation, mRNA storage and stabilization and cell signalling, during stress. One defining feature of SGs is their dynamism, as they are quickly assembled upon stress and then rapidly dispersed after the stress source is no longer present. Recently, SGs dynamics, their components and their functions have begun to be studied in the context of human diseases. Interestingly, the regulated protein self-assembly that mediates SG formation contrasts with the pathological protein aggregation that is a feature of several neurodegenerative diseases. In particular, aberrant protein coalescence is a key feature of polyglutamine (PolyQ) diseases, a group of nine disorders that are caused by an abnormal expansion of PolyQ tract-bearing proteins, which increases the propensity of those proteins to aggregate. Available data concerning the abnormal properties of the mutant PolyQ disease-causing proteins and their involvement in stress response dysregulation strongly suggests an important role for SGs in the pathogenesis of PolyQ disorders. This review aims at discussing the evidence supporting the existence of a link between SGs functionality and PolyQ disorders, by focusing on the biology of SGs and on the way it can be altered in a PolyQ disease context. |
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Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?Spinocerebellar ataxia type-3N-terminal huntingtinOxidative stressMutant huntingtinCellular stressMolecular-mechanismsNuclear inclusionsAndrogen receptorAxonal-transportPhase-transitionStress granules (SGs) are membraneless cell compartments formed in response to different stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other proteins coalesce together. SGs assembly is crucial for cell survival, since SGs are implicated in the regulation of translation, mRNA storage and stabilization and cell signalling, during stress. One defining feature of SGs is their dynamism, as they are quickly assembled upon stress and then rapidly dispersed after the stress source is no longer present. Recently, SGs dynamics, their components and their functions have begun to be studied in the context of human diseases. Interestingly, the regulated protein self-assembly that mediates SG formation contrasts with the pathological protein aggregation that is a feature of several neurodegenerative diseases. In particular, aberrant protein coalescence is a key feature of polyglutamine (PolyQ) diseases, a group of nine disorders that are caused by an abnormal expansion of PolyQ tract-bearing proteins, which increases the propensity of those proteins to aggregate. Available data concerning the abnormal properties of the mutant PolyQ disease-causing proteins and their involvement in stress response dysregulation strongly suggests an important role for SGs in the pathogenesis of PolyQ disorders. This review aims at discussing the evidence supporting the existence of a link between SGs functionality and PolyQ disorders, by focusing on the biology of SGs and on the way it can be altered in a PolyQ disease context.ALG-01-0145-FEDER-29480, SFRH/BD/133192/2017, SFRH/BD/133192/2017, SFRH/BD/148533/2019Springer NatureSapientiaMarcelo, AdrianaKoppenol, RebekahAlmeida, Luis PedroMatos, Carlos ANóbrega, Clévio2021-07-07T09:22:34Z2021-062021-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/16735eng2041-488910.1038/s41419-021-03873-8info: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:RCAAP2023-07-24T10:28:43Zoai:sapientia.ualg.pt:10400.1/16735Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:06:48.505451Repositório 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 |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
title |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
spellingShingle |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? Marcelo, Adriana Spinocerebellar ataxia type-3 N-terminal huntingtin Oxidative stress Mutant huntingtin Cellular stress Molecular-mechanisms Nuclear inclusions Androgen receptor Axonal-transport Phase-transition |
title_short |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
title_full |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
title_fullStr |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
title_full_unstemmed |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
title_sort |
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? |
author |
Marcelo, Adriana |
author_facet |
Marcelo, Adriana Koppenol, Rebekah Almeida, Luis Pedro Matos, Carlos A Nóbrega, Clévio |
author_role |
author |
author2 |
Koppenol, Rebekah Almeida, Luis Pedro Matos, Carlos A Nóbrega, Clévio |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Marcelo, Adriana Koppenol, Rebekah Almeida, Luis Pedro Matos, Carlos A Nóbrega, Clévio |
dc.subject.por.fl_str_mv |
Spinocerebellar ataxia type-3 N-terminal huntingtin Oxidative stress Mutant huntingtin Cellular stress Molecular-mechanisms Nuclear inclusions Androgen receptor Axonal-transport Phase-transition |
topic |
Spinocerebellar ataxia type-3 N-terminal huntingtin Oxidative stress Mutant huntingtin Cellular stress Molecular-mechanisms Nuclear inclusions Androgen receptor Axonal-transport Phase-transition |
description |
Stress granules (SGs) are membraneless cell compartments formed in response to different stress stimuli, wherein translation factors, mRNAs, RNA-binding proteins (RBPs) and other proteins coalesce together. SGs assembly is crucial for cell survival, since SGs are implicated in the regulation of translation, mRNA storage and stabilization and cell signalling, during stress. One defining feature of SGs is their dynamism, as they are quickly assembled upon stress and then rapidly dispersed after the stress source is no longer present. Recently, SGs dynamics, their components and their functions have begun to be studied in the context of human diseases. Interestingly, the regulated protein self-assembly that mediates SG formation contrasts with the pathological protein aggregation that is a feature of several neurodegenerative diseases. In particular, aberrant protein coalescence is a key feature of polyglutamine (PolyQ) diseases, a group of nine disorders that are caused by an abnormal expansion of PolyQ tract-bearing proteins, which increases the propensity of those proteins to aggregate. Available data concerning the abnormal properties of the mutant PolyQ disease-causing proteins and their involvement in stress response dysregulation strongly suggests an important role for SGs in the pathogenesis of PolyQ disorders. This review aims at discussing the evidence supporting the existence of a link between SGs functionality and PolyQ disorders, by focusing on the biology of SGs and on the way it can be altered in a PolyQ disease context. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-07-07T09:22:34Z 2021-06 2021-06-01T00:00:00Z |
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/10400.1/16735 |
url |
http://hdl.handle.net/10400.1/16735 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
2041-4889 10.1038/s41419-021-03873-8 |
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 |
Springer Nature |
publisher.none.fl_str_mv |
Springer Nature |
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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1799133311158714368 |