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Biomolecules. 2015 Apr 14;5(2):412-34. doi: 10.3390/biom5020412.

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

Author information

1
Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8548, USA. Zhong.Shen@UTsouthwestern.edu.
2
Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8548, USA. James.Malter@UTsouthwestern.edu.

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.

PMID:
25874604
PMCID:
PMC4496679
DOI:
10.3390/biom5020412
[Indexed for MEDLINE]
Free PMC Article

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