Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/103825
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Marcelo, Adriana | - |
dc.contributor.author | Koppenol, Rebekah | - |
dc.contributor.author | Almeida, Luís Pereira de | - |
dc.contributor.author | Matos, Carlos A. | - |
dc.contributor.author | Nóbrega, Clévio | - |
dc.date.accessioned | 2022-11-30T10:24:00Z | - |
dc.date.available | 2022-11-30T10:24:00Z | - |
dc.date.issued | 2021-06-08 | - |
dc.identifier.issn | 2041-4889 | pt |
dc.identifier.uri | https://hdl.handle.net/10316/103825 | - |
dc.description.abstract | 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. | pt |
dc.language.iso | eng | pt |
dc.publisher | Springer Nature | pt |
dc.relation | FCT - project ALG-01- 0145-FEDER-29480) “SeGrPolyQ”, with CRESC ALGARVE 2020 cofounding, the French Muscular Dystrophy Association (AFM-Téléthon) project #22424 and by the Ataxia UK (ZUNIALGA project | pt |
dc.relation | FCT - Ph.D. fellowship SFRH/BD/133192/2017 | pt |
dc.relation | FCT - Ph.D. fellowship SFRH/BD/148533/2019 | pt |
dc.rights | openAccess | pt |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | pt |
dc.subject.mesh | Animals | pt |
dc.subject.mesh | Cytoplasmic Granules | pt |
dc.subject.mesh | Humans | pt |
dc.subject.mesh | Neurodegenerative Diseases | pt |
dc.subject.mesh | Peptides | pt |
dc.subject.mesh | Protein Aggregation, Pathological | pt |
dc.subject.mesh | RNA-Binding Proteins | pt |
dc.subject.mesh | Signal Transduction | pt |
dc.subject.mesh | Stress, Physiological | pt |
dc.title | Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation? | pt |
dc.type | article | - |
degois.publication.firstPage | 592 | pt |
degois.publication.issue | 6 | pt |
degois.publication.title | Cell Death and Disease | pt |
dc.peerreviewed | yes | pt |
dc.identifier.doi | 10.1038/s41419-021-03873-8 | pt |
degois.publication.volume | 12 | pt |
dc.date.embargo | 2021-06-08 | * |
uc.date.periodoEmbargo | 0 | pt |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en | - |
item.openairetype | article | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | Com Texto completo | - |
crisitem.author.researchunit | CNC - Center for Neuroscience and Cell Biology | - |
crisitem.author.researchunit | CNC - Center for Neuroscience and Cell Biology | - |
crisitem.author.researchunit | CIBB - Center for Innovative Biomedicine and Biotechnology | - |
crisitem.author.researchunit | CNC - Center for Neuroscience and Cell Biology | - |
crisitem.author.orcid | 0000-0002-7327-0170 | - |
crisitem.author.orcid | 0000-0001-5831-3307 | - |
crisitem.author.orcid | 0000-0002-8312-5292 | - |
Appears in Collections: | I&D CNC - Artigos em Revistas Internacionais FFUC- Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Stress-granules-RNAbinding-proteins-and-polyglutamine-diseases-too-much-aggregationCell-Death-and-Disease.pdf | 1.62 MB | Adobe PDF | View/Open |
Page view(s)
73
checked on May 8, 2024
Download(s)
26
checked on May 8, 2024
Google ScholarTM
Check
Altmetric
Altmetric
This item is licensed under a Creative Commons License