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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Quaresma, Alexandre J. C. [1] ; Bressan, G. C. [1, 2] ; Gava, L. M. [3, 2] ; Lanza, D. C. F. [2, 1] ; Ramos, C. H. I. [3] ; Kobarg, Joerg [1, 2]
Total Authors: 6
Affiliation:
[1] LNLS, Brazilian Synchrotron Light Lab, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol, BR-13083970 Campinas, SP - Brazil
[3] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Experimental Cell Research; v. 315, n. 6, p. 968-980, APR 1 2009.
Web of Science Citations: 23
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. (AU)

FAPESP's process: 05/00235-1 - Functional and structural studies of three human regulatory proteins: Fez1, Ki-1/57 and NSAP1 (hnRNP-Q)
Grantee:Jörg Kobarg
Support type: Regular Research Grants