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Feedback Regulation of Kinase Signaling Pathways by AREs and GREs

In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abu...

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Autores principales: Vlasova-St. Louis, Irina, Bohjanen, Paul R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810089/
https://www.ncbi.nlm.nih.gov/pubmed/26821046
http://dx.doi.org/10.3390/cells5010004
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author Vlasova-St. Louis, Irina
Bohjanen, Paul R.
author_facet Vlasova-St. Louis, Irina
Bohjanen, Paul R.
author_sort Vlasova-St. Louis, Irina
collection PubMed
description In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs, and affect gene expression during cellular activation, proliferation, and stress responses. In this review, we summarize the effect of phosphorylation on the function of ARE-binding proteins ZFP36 and ELAVL1 and the GRE-binding protein CELF1. The networks of target mRNAs that these proteins bind and regulate include transcripts encoding kinases and kinase signaling pathways (KSP) components. Thus, kinase signaling pathways are involved in feedback regulation, whereby kinases regulate RNA-binding proteins that subsequently regulate mRNA stability of ARE- or GRE-containing transcripts that encode components of KSP.
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spelling pubmed-48100892016-04-04 Feedback Regulation of Kinase Signaling Pathways by AREs and GREs Vlasova-St. Louis, Irina Bohjanen, Paul R. Cells Review In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs, and affect gene expression during cellular activation, proliferation, and stress responses. In this review, we summarize the effect of phosphorylation on the function of ARE-binding proteins ZFP36 and ELAVL1 and the GRE-binding protein CELF1. The networks of target mRNAs that these proteins bind and regulate include transcripts encoding kinases and kinase signaling pathways (KSP) components. Thus, kinase signaling pathways are involved in feedback regulation, whereby kinases regulate RNA-binding proteins that subsequently regulate mRNA stability of ARE- or GRE-containing transcripts that encode components of KSP. MDPI 2016-01-25 /pmc/articles/PMC4810089/ /pubmed/26821046 http://dx.doi.org/10.3390/cells5010004 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Vlasova-St. Louis, Irina
Bohjanen, Paul R.
Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title_full Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title_fullStr Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title_full_unstemmed Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title_short Feedback Regulation of Kinase Signaling Pathways by AREs and GREs
title_sort feedback regulation of kinase signaling pathways by ares and gres
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810089/
https://www.ncbi.nlm.nih.gov/pubmed/26821046
http://dx.doi.org/10.3390/cells5010004
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