Cataloguing the phosphorylation sites of tristetraprolin (TTP): Functional implications for inflammatory diseases.

Rezcallah, MC; Al-Mazi, T; Ammit, AJ

Cataloguing the phosphorylation sites of tristetraprolin (TTP): Functional implications for inflammatory diseases.

Rezcallah, MC Al-Mazi, T Ammit, AJ

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Publisher:: Elsevier
Publication Type:: Journal Article
Citation:: Cellular Signalling, 2021, 78, pp. 1-12
Issue Date:: 2021-02

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Field	Value	Language
dc.contributor.author	Rezcallah, MC
dc.contributor.author	Al-Mazi, T
dc.contributor.author	Ammit, AJ
dc.date.accessioned	2021-01-04T22:52:18Z
dc.date.available	2020-11-29
dc.date.available	2021-01-04T22:52:18Z
dc.date.issued	2021-02
dc.identifier.citation	Cellular Signalling, 2021, 78, pp. 1-12
dc.identifier.issn	0898-6568
dc.identifier.issn	1873-3913
dc.identifier.uri	http://hdl.handle.net/10453/145071
dc.description.abstract	Tristetraprolin (TTP) is a destabilizing mRNA binding protein known to regulate gene expression of a wide variety of targets, including those that control inflammation. TTP expression, regulation and function is controlled by phosphorylation. While the importance of key serine (S) sites (S<sup>52</sup> and S<sup>178</sup> in mice and S<sup>186</sup> in humans) has been recognized, other sites on the hyperphosphorylated TTP protein have more recently emerged as playing an important role in regulating cellular signalling and downstream functions of TTP. In order to propel investigation of TTP and fully exploit its potential as a drug target in inflammatory disease, this review will catalogue TTP phosphorylation sites in both the murine and human TTP protein, the known and unknown roles and functions of these sites, the kinases and phosphatases that act upon TTP and overview methodological approaches to increase our knowledge of this important protein regulated by phosphorylation.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	Elsevier
dc.relation	The Rebecca L Cooper Medical Research Foundation L1141365
dc.relation.ispartof	Cellular Signalling
dc.relation.isbasedon	10.1016/j.cellsig.2020.109868
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	0601 Biochemistry and Cell Biology, 1116 Medical Physiology
dc.subject.classification	Biochemistry & Molecular Biology
dc.title	Cataloguing the phosphorylation sites of tristetraprolin (TTP): Functional implications for inflammatory diseases.
dc.type	Journal Article
utslib.citation.volume	78
utslib.location.activity	England
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	1116 Medical Physiology
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	closed_access	*
pubs.consider-herdc	false
dc.date.updated	2021-01-04T22:52:10Z
pubs.publication-status	Published
pubs.volume	78

Abstract:

Tristetraprolin (TTP) is a destabilizing mRNA binding protein known to regulate gene expression of a wide variety of targets, including those that control inflammation. TTP expression, regulation and function is controlled by phosphorylation. While the importance of key serine (S) sites (S⁵² and S¹⁷⁸ in mice and S¹⁸⁶ in humans) has been recognized, other sites on the hyperphosphorylated TTP protein have more recently emerged as playing an important role in regulating cellular signalling and downstream functions of TTP. In order to propel investigation of TTP and fully exploit its potential as a drug target in inflammatory disease, this review will catalogue TTP phosphorylation sites in both the murine and human TTP protein, the known and unknown roles and functions of these sites, the kinases and phosphatases that act upon TTP and overview methodological approaches to increase our knowledge of this important protein regulated by phosphorylation.

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http://hdl.handle.net/10453/145071