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10.1042/BST20160166

http://scihub22266oqcxt.onion/10.1042/BST20160166
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C5095909!5095909!27911715
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suck abstract from ncbi


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pmid27911715      Biochem+Soc+Trans 2016 ; 44 (5): 1321-37
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  • The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases #MMPMID27911715
  • Clark AR; Dean JL
  • Biochem Soc Trans 2016[Oct]; 44 (5): 1321-37 PMID27911715show ga
  • 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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