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/10316/103825 https://doi.org/10.1038/s41419-021-03873-8 |
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?AnimalsCytoplasmic GranulesHumansNeurodegenerative DiseasesPeptidesProtein Aggregation, PathologicalRNA-Binding ProteinsSignal TransductionStress, PhysiologicalStress 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.Springer Nature2021-06-08info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/103825http://hdl.handle.net/10316/103825https://doi.org/10.1038/s41419-021-03873-8eng2041-4889Marcelo, AdrianaKoppenol, RebekahAlmeida, Luís Pereira deMatos, Carlos A.Nóbrega, Clévioinfo: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:RCAAP2022-11-30T21:38:31Zoai:estudogeral.uc.pt:10316/103825Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:20:35.752315Repositório 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 Animals Cytoplasmic Granules Humans Neurodegenerative Diseases Peptides Protein Aggregation, Pathological RNA-Binding Proteins Signal Transduction Stress, Physiological |
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, Luís Pereira de Matos, Carlos A. Nóbrega, Clévio |
author_role |
author |
author2 |
Koppenol, Rebekah Almeida, Luís Pereira de Matos, Carlos A. Nóbrega, Clévio |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Marcelo, Adriana Koppenol, Rebekah Almeida, Luís Pereira de Matos, Carlos A. Nóbrega, Clévio |
dc.subject.por.fl_str_mv |
Animals Cytoplasmic Granules Humans Neurodegenerative Diseases Peptides Protein Aggregation, Pathological RNA-Binding Proteins Signal Transduction Stress, Physiological |
topic |
Animals Cytoplasmic Granules Humans Neurodegenerative Diseases Peptides Protein Aggregation, Pathological RNA-Binding Proteins Signal Transduction Stress, Physiological |
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 |
2021-06-08 |
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/10316/103825 http://hdl.handle.net/10316/103825 https://doi.org/10.1038/s41419-021-03873-8 |
url |
http://hdl.handle.net/10316/103825 https://doi.org/10.1038/s41419-021-03873-8 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
2041-4889 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Springer Nature |
publisher.none.fl_str_mv |
Springer Nature |
dc.source.none.fl_str_mv |
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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 |
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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) |
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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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1799134098366660608 |