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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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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. |
format | Online Article Text |
id | pubmed-4810089 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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