Human hnRNP Q re-localizes to cytoplasmic granules upon PMA, thapsigargin, arsenite and heat-shock treatments

dc.creatorQuaresma, AJC
dc.creatorBressan, GC
dc.creatorGava, LM
dc.creatorLanza, DCF
dc.creatorRamos, CHI
dc.creatorKobarg, J
dc.date2009
dc.dateAPR 1
dc.date2014-11-14T09:06:28Z
dc.date2015-11-26T16:05:32Z
dc.date2014-11-14T09:06:28Z
dc.date2015-11-26T16:05:32Z
dc.date.accessioned2018-03-28T22:54:30Z
dc.date.available2018-03-28T22:54:30Z
dc.identifierExperimental Cell Research. Elsevier Inc, v. 315, n. 6, n. 968, n. 980, 2009.
dc.identifier0014-4827
dc.identifierWOS:000264586500006
dc.identifier10.1016/j.yexcr.2009.01.012
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/68906
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/68906
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/68906
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1265727
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionEukaryotic gene expression is regulated on different levels ranging from pre-mRNA processing to translation. One of the most characterized families of RNA-binding proteins is the group of hnRNPs: heterogenous nuclear ribonucleoproteins. Members of this protein family play important roles in gene expression control and mRNAs metabolism. In the cytoplasm, several hnRNPs proteins are involved in RNA-related processes and they can be frequently found in two specialized structures, known as GW-bodies (GWbs), previously known as processing bodies: PBs, and stress granules, which may be formed in response to specific stimuli. GWbs have been early reported to be involved in the mRNA decay process, acting as a site of mRNA degradation. In a similar way, stress granules (SGs) have been described as cytoplasmic aggregates, which contain accumulated mRNAs in cells under stress conditions and present reduced or inhibited translation. Here, we characterized the hnRNP Q localization after different stress conditions. hnRNP Q is a predominantly nuclear protein that exhibits a modular organization and several RNA-related functions. Our data suggest that the nuclear localization of hnRNP Q might be modified after different treatments, such as: PMA, thapsigargin, arsenite and heat shock. Under different stress conditions, hnRNP Q can fully co-localize with the endoplasmatic reticulum specific chaperone, BiP. However, under stress, this protein only co-localizes partially with the proteins: GW182 - GWbs marker protein and TIA-1 stress granule component. (C) 2009 Elsevier Inc. All rights reserved.
dc.description315
dc.description6
dc.description968
dc.description980
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionLNLS
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [05/00235-1]
dc.languageen
dc.publisherElsevier Inc
dc.publisherSan Diego
dc.publisherEUA
dc.relationExperimental Cell Research
dc.relationExp. Cell Res.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectProtein-protein interactions
dc.subjectStress granules
dc.subjectProtein bodies
dc.subjectSub cellular localization
dc.subjectProtein-kinase-c
dc.subjectMessenger-rna Decay
dc.subjectChain Binding-protein
dc.subjectMammalian Stress Granules
dc.subjectDetermining Gene-product
dc.subjectRibosomal Entry Site
dc.subjectProcessing Bodies
dc.subjectInteracting Protein
dc.subjectGry-rbp
dc.subjectApoptosis
dc.titleHuman hnRNP Q re-localizes to cytoplasmic granules upon PMA, thapsigargin, arsenite and heat-shock treatments
dc.typeArtículos de revistas


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