{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cairrao F"],"funding":["&quot;la Caixa&quot; Foundation"],"pagination":["1587"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8948244"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_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<sup>unspliced</sup> and Xbp1<sup>spliced</sup> mRNAs, but only Xbp1<sup>spliced</sup> is stabilized by Pumilio. Furthermore, Pumilio displays Ire1 kinase-dependent phosphorylation during ER stres"],"journal":["Nature communications"],"pubmed_title":["Pumilio protects Xbp1 mRNA from regulated Ire1-dependent decay."],"pmcid":["PMC8948244"],"funding_grant_id":["LCF/PR/HR17/52150018"],"pubmed_authors":["Le Thomas A","Marsters S","Ashkenazi A","Cairrao F","Santos CC","Domingos PM"],"additional_accession":[]},"is_claimable":false,"name":"Pumilio protects Xbp1 mRNA from regulated Ire1-dependent decay.","description":"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<sup>unspliced</sup> and Xbp1<sup>spliced</sup> mRNAs, but only Xbp1<sup>spliced</sup> is stabilized by Pumilio. Furthermore, Pumilio displays Ire1 kinase-dependent phosphorylation during ER stres","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-19T00:41:28.558Z","creation":"2025-04-07T11:45:31.556Z"},"accession":"S-EPMC8948244","cross_references":{"pubmed":["35332141"],"doi":["10.1038/s41467-022-29105-x"]}}