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      The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases

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          Abstract

          Twenty years ago, the first description of a tristetraprolin (TTP) knockout mouse highlighted the fundamental role of TTP in the restraint of inflammation. Since then, work from several groups has generated a detailed picture of the expression and function of TTP. It is a sequence-specific RNA-binding protein that orchestrates the deadenylation and degradation of several mRNAs encoding inflammatory mediators. It is very extensively post-translationally modified, with more than 30 phosphorylations that are supported by at least two independent lines of evidence. The phosphorylation of two particular residues, serines 52 and 178 of mouse TTP (serines 60 and 186 of the human orthologue), has profound effects on the expression, function and localisation of TTP. Here, we discuss the control of TTP biology via its phosphorylation and dephosphorylation, with a particular focus on recent advances and on questions that remain unanswered.

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          Mitogen-activated protein kinases in innate immunity.

          J. Simon C. Arthur, Steven C Ley (2013)
          Following pathogen infection or tissue damage, the stimulation of pattern recognition receptors on the cell surface and in the cytoplasm of innate immune cells activates members of each of the major mitogen-activated protein kinase (MAPK) subfamilies--the extracellular signal-regulated kinase (ERK), p38 and Jun N-terminal kinase (JNK) subfamilies. In conjunction with the activation of nuclear factor-κB and interferon-regulatory factor transcription factors, MAPK activation induces the expression of multiple genes that together regulate the inflammatory response. In this Review, we discuss our current knowledge about the regulation and the function of MAPKs in innate immunity, as well as the importance of negative feedback loops in limiting MAPK activity to prevent host tissue damage. We also examine how pathogens have evolved complex mechanisms to manipulate MAPK activation to increase their virulence. Finally, we consider the potential of the pharmacological targeting of MAPK pathways to treat autoimmune and inflammatory diseases.
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            HuR and mRNA stability.

            C. M. Brennan, J. Steitz* (2001)
            An important mechanism of posttranscriptional gene regulation in mammalian cells is the rapid degradation of messenger RNAs (mRNAs) signaled by AU-rich elements (AREs) in their 3' untranslated regions. HuR, a ubiquitously expressed member of the Hu family of RNA-binding proteins related to Drosophila ELAV, selectively binds AREs and stabilizes ARE-containing mRNAs when overexpressed in cultured cells. This review discusses mRNA decay as a general form of gene regulation, decay signaled by AREs, and the role of HuR and its Hu-family relatives in antagonizing this mRNA degradation pathway. The influence of newly identified protein ligands to HuR on HuR function in both normal and stressed cells may explain how ARE-mediated mRNA decay is regulated in response to environmental change.
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              Tristetraprolin (TTP): interactions with mRNA and proteins, and current thoughts on mechanisms of action.

              Seth A Brooks, Perry Blackshear (2015)
              Changes in mRNA stability and translation are critical control points in the regulation of gene expression, particularly genes encoding growth factors, inflammatory mediators, and proto-oncogenes. Adenosine and uridine (AU)-rich elements (ARE), often located in the 3' untranslated regions (3'UTR) of mRNAs, are known to target transcripts for rapid decay. They are also involved in the regulation of mRNA stability and translation in response to extracellular cues. This review focuses on one of the best characterized ARE binding proteins, tristetraprolin (TTP), the founding member of a small family of CCCH tandem zinc finger proteins. In this survey, we have reviewed the current status of TTP interactions with mRNA and proteins, and discussed current thinking about TTP's mechanism of action to promote mRNA decay. We also review the proposed regulation of TTP's functions by phosphorylation. Finally, we have discussed emerging evidence for TTP operating as a translational regulator. This article is part of a Special Issue entitled: RNA Decay mechanisms. Published by Elsevier B.V.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Biochem Soc Trans
                Journal ID (iso-abbrev): Biochem. Soc. Trans
                Journal ID (hwp): ppbiost
                Journal ID (publisher-id): BST
                Title: Biochemical Society Transactions
                Publisher: Portland Press Ltd.
                ISSN (Print): 0300-5127
                ISSN (Electronic): 1470-8752
                Publication date (Print): 15 October 2016
                Publication date (Electronic): 19 October 2016
                Volume: 44
                Issue: 5
                Pages: 1321-1337
                Affiliations
                [1 ]Institute of Inflammation and Ageing, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, U.K.
                [2 ]Kennedy Institute of Rheumatology, University of Oxford, Oxford OX3 7FY, U.K.
                Author notes
                Correspondence: Andrew R. Clark ( a.r.clark@ 123456bham.ac.uk )
                Article
                Publisher ID: BST-2016-0166
                DOI: 10.1042/BST20160166
                PMC ID: 5095909
                PubMed ID: 27911715
                SO-VID: c05f6d16-d327-4b0d-97fd-0cc31b807888
                Copyright © © 2016 The Author(s)
                License:

                This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).

                History
                Date received : 9 June 2016
                Date revision received : 25 July 2016
                Date accepted : 28 July 2016
                Categories
                Subject: Phosphatases and Signalling in Health and Disease
                Subject: 3
                Subject: 45
                Subject: 16
                Subject: 13

                ScienceOpen disciplines: Biochemistry
                Keywords: dual-specificity phosphatases,mapk p38,mrna stability,pp2a,tristetraprolin
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: dual-specificity phosphatases, mapk p38, mrna stability, pp2a, tristetraprolin

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