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Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress

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dc.contributor.author Solé, Carme
dc.contributor.author Nadal Ribelles, Mariona, 1984-
dc.contributor.author Kraft, Claudine
dc.contributor.author Peter, Matthias
dc.contributor.author Posas Garriga, Francesc
dc.contributor.author Nadal Clanchet, Eulàlia de
dc.date.accessioned 2015-12-17T15:44:29Z
dc.date.available 2015-12-17T15:44:29Z
dc.date.issued 2011
dc.identifier.citation Solé C, Nadal-Ribelles M, Kraft C, Peter M, Posas F, de Nadal E. Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress. EMBO journal. 2011;30(16):3274-84. DOI: 10.1038/emboj.2011.227
dc.identifier.issn 0261-4189
dc.identifier.uri http://hdl.handle.net/10230/25459
dc.description.abstract Protein ubiquitylation is a key process in the regulation of many cellular processes. The balance between the activity of ubiquitin ligases and that of proteases controls the level of ubiquitylation. In response to extracellular stimuli, stress-activated protein kinases (SAPK) modulate gene expression to maximize cell survival. In yeast, the Hog1 SAPK has a key role in reprogramming the gene expression pattern required for cell survival upon osmostress. Here, we show that the Ubp3 ubiquitin protease is a target for the Hog1 SAPK to modulate gene expression. ubp3 mutant cells are defective in expression of osmoresponsive genes. Hog1 interacts with and phosphorylates Ubp3 at serine 695, which is essential to determine the extent of transcriptional activation in response to osmostress. Furthermore, Ubp3 is recruited to osmoresponsive genes to modulate transcriptional initiation as well as elongation. Therefore, Ubp3 activity responds to external stimuli and is required for transcriptional activation upon osmostress.
dc.description.sponsorship MN is the recipient of an FIS (Spanish Government) fellowship and FP is the recipient of an ICREA Acadèmia (Generalitat de Catalunya). This work was supported by Fundación Marcelino Botín (FMB) and grants from the Spanish Ministry of Science and Innovation (BFU2008-00530 to EN and BIO2009-07762 to FP) and the FP7 (UNICELLSYS) framework programme.
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Nature Publishing Group
dc.relation.ispartof EMBO journal. 2011;30(16):3274-84
dc.rights © Nature Publishing Group. http://dx.doi.org/10.1038/emboj.2011.227. This work is licensed under a Creative Commons Attribution-NonCommercial-Share Alike 3.0 Unported licence
dc.rights.uri http://creativecommons.org/licenses/by-nc-sa/3.0/
dc.subject.other RNA missatger
dc.subject.other Saccharomyces cerevisiae -- Metabolisme
dc.subject.other Endopeptidases -- Fisiologia patològica
dc.title Control of Ubp3 ubiquitin protease activity by the Hog1 SAPK modulates transcription upon osmostress
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1038/emboj.2011.227
dc.subject.keyword Gene expression
dc.subject.keyword Hog1
dc.subject.keyword Osmostress
dc.subject.keyword SAPK
dc.subject.keyword Ubp3
dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/201142
dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BFU2008-00530
dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2009-07762
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion


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