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Biomolecules 2015, 5(2), 412-434; doi:10.3390/biom5020412

Regulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1

Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8548, USA
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Academic Editor: André P. Gerber
Received: 4 March 2015 / Revised: 23 March 2015 / Accepted: 31 March 2015 / Published: 14 April 2015
(This article belongs to the Special Issue RNA-Binding Proteins—Structure, Function, Networks and Disease)
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Abstract

The accumulation of 3' untranslated region (3'-UTR), AU-rich element (ARE) containing mRNAs, are predominantly controlled at the post-transcriptional level. Regulation appears to rely on a variable and dynamic interaction between mRNA target and ARE-specific binding proteins (AUBPs). The AUBP-ARE mRNA recognition is directed by multiple intracellular signals that are predominantly targeted at the AUBPs. These include (but are unlikely limited to) methylation, acetylation, phosphorylation, ubiquitination and isomerization. These regulatory events ultimately affect ARE mRNA location, abundance, translation and stability. In this review, we describe recent advances in our understanding of phosphorylation and its impact on conformation of the AUBPs, interaction with ARE mRNAs and highlight the role of Pin1 mediated prolyl cis-trans isomerization in these biological process. View Full-Text
Keywords: AU-rich element; phosphorylation; prolyl isomerase Pin1; RNA-binding protein; signaling; gene regulation; mRNA turnover; kinase AU-rich element; phosphorylation; prolyl isomerase Pin1; RNA-binding protein; signaling; gene regulation; mRNA turnover; kinase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Shen, Z.-J.; Malter, J.S. Regulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1. Biomolecules 2015, 5, 412-434.

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