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Type: Artigo de periódico
Title: Human hnRNP Q re-localizes to cytoplasmic granules upon PMA, thapsigargin, arsenite and heat-shock treatments
Author: Quaresma, AJC
Bressan, GC
Gava, LM
Lanza, DCF
Ramos, CHI
Kobarg, J
Abstract: Eukaryotic 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.
Subject: Protein-protein interactions
Stress granules
Protein bodies
Sub cellular localization
Country: EUA
Editor: Elsevier Inc
Citation: Experimental Cell Research. Elsevier Inc, v. 315, n. 6, n. 968, n. 980, 2009.
Rights: fechado
Identifier DOI: 10.1016/j.yexcr.2009.01.012
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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