The stress-induced heat shock protein 70.3 expression is regulated by a dual-component mechanism involving alternative polyadenylation and HuR

Biochimica Et Biophysica Acta
Stephen M KraynikMichael Tranter

Abstract

Heat shock protein 70.3 (Hsp70.3) expression increases in response to cellular stress and plays a cytoprotective role. We have previously shown that Hsp70.3 expression is controlled through coordinated post-transcriptional regulation by miRNAs and alternative polyadenylation (APA), and APA-mediated shortening of the Hsp70.3 3'-UTR facilitates increased protein expression. A stress-induced increase in Hsp70.3 mRNA and protein expression is accompanied by alternative polyadenylation (APA)-mediated truncation of the 3'UTR of the Hsp70.3 mRNA transcript. However, the role that APA plays in stress-induced expression of Hsp70.3 remains unclear. Our results show that APA-mediated truncation of the Hsp70.3 3'UTR increases protein expression through enhanced polyribosome loading. Additionally, we demonstrate that the RNA binding protein HuR, which has been previously shown to play a role in mediating APA, is necessary for heat shock mediated increase in Hsp70.3 mRNA and protein. However, it is somewhat surprising to note that HuR does not play a role in APA of the Hsp70.3 mRNA, and these two regulatory events appear to be mutually exclusive regulators of Hsp70.3 expression. These results not only provide important insight to the regulat...Continue Reading

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Citations

Dec 1, 2017·American Journal of Hypertension·Roopesh S GangwarJeffrey A Deiuliis
Oct 12, 2018·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Incheol RyuYoon Ki Kim
May 3, 2019·Wiley Interdisciplinary Reviews. RNA·Jason SadekImed Eddine Gallouzi
Jan 18, 2017·Wiley Interdisciplinary Reviews. RNA·Donald J DeGracia
Oct 28, 2019·Wiley Interdisciplinary Reviews. RNA·Michael Robert Murphy, Frida Esther Kleiman
Sep 29, 2021·Wiley Interdisciplinary Reviews. RNA·Neeraja K MohananRakesh S Laishram

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