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2013 ; 1829
(6-7
): 666-79
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Tristetraprolin (TTP): interactions with mRNA and proteins, and current thoughts
on mechanisms of action
#MMPMID23428348
Brooks SA
; Blackshear PJ
Biochim Biophys Acta
2013[Jun]; 1829
(6-7
): 666-79
PMID23428348
show ga
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.