Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 278, Issue 35, Pages 33039-33048Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M305775200
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- NCI NIH HHS [R01 CA52443] Funding Source: Medline
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Messenger RNA turnover directed by A+U-rich elements (AREs) involves selected ARE-binding proteins. Whereas several signaling systems may modulate ARE-directed mRNA decay and/or post-translationally modify specific trans-acting factors, it is unclear how these mechanisms are linked. In THP-1 monocytic leukemia cells, phorbol ester-induced stabilization of some mRNAs containing AREs was accompanied by dephosphorylation of Ser(83) and Ser(87) of polysome-associated p40(AUF1). Here, we report that phosphorylation of p40(AUF1) influences its ARE-binding affinity as well as the RNA conformational dynamics and global structure of the p40(AUF1)-ARE ribonucleoprotein complex. Most notably, association of unphosphorylated p40(AUF1) induces a condensed RNA conformation upon ARE substrates. By contrast, phosphorylation of p40(AUF1) at Ser(83) and Ser(87) inhibits this RNA structural transition. These data indicate that selective AUF1 phosphorylation may regulate ARE-directed mRNA turnover by remodeling local RNA structures, thus potentially altering the presentation of RNA and/or protein determinants involved in subsequent trans-factor recruitment.
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