Pumilio protects Xbp1 mRNA from regulated Ire1-dependent decay.

ABSTRACT: The unfolded protein response (UPR) maintains homeostasis of the endoplasmic reticulum (ER). Residing in the ER membrane, the UPR mediator Ire1 deploys its cytoplasmic kinase-endoribonuclease domain to activate the key UPR transcription factor Xbp1 through non-conventional splicing of Xbp1 mRNA. Ire1 also degrades diverse ER-targeted mRNAs through regulated Ire1-dependent decay (RIDD), but how it spares Xbp1 mRNA from this decay is unknown. Here, we identify binding sites for the RNA-binding protein Pumilio in the 3'UTR Drosophila Xbp1. In the developing Drosophila eye, Pumilio binds both the Xbp1^unspliced and Xbp1^spliced mRNAs, but only Xbp1^spliced is stabilized by Pumilio. Furthermore, Pumilio displays Ire1 kinase-dependent phosphorylation during ER stres

SUBMITTER: Cairrao F 

PROVIDER: S-EPMC8948244 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature