{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Georgiou M"],"funding":["European Research Council","Fight for Sight","Retina UK","NIMAD","National Institute for Medical Research Development","MRC UK"],"pagination":["e759"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8926896"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(3)"],"pubmed_abstract":["<h4>Introduction</h4>Mutations in pre-mRNA processing factor 31 (PRPF31), a core protein of the spliceosomal tri-snRNP complex, cause autosomal-dominant retinitis pigmentosa (adRP). It has remained an enigma why mutations in ubiquitously expressed tri-snRNP proteins result in retina-specific disorders, and so far, the underlying mechanism of splicing factors-related RP is poorly understood.<h4>Methods</h4>We used the induced pluripotent stem cell (iPSC) technology to generate retinal organoids and RPE models from four patients with severe and very severe PRPF31-adRP, unaffected individuals and a CRISPR/Cas9 isogenic control.<h4>Results</h4>To fully assess the impacts of PRPF31 mutations, quantitative proteomics analyses of retinal organoids and RPE cells were carried out showing RNA splici"],"journal":["Clinical and translational medicine"],"pubmed_title":["Activation of autophagy reverses progressive and deleterious protein aggregation in PRPF31 patient-induced pluripotent stem cell-derived retinal pigment epithelium cells."],"pmcid":["PMC8926896"],"funding_grant_id":["1456/1457","CoG_614620","GR584","GR595","614620","MR/T017503/1","989278"],"pubmed_authors":["Pan KT","Armstrong L","Urlaub H","Ludwig SEJ","Luhrmann R","Buskin A","Korolchuk V","Collin J","Al-Aama J","Yang C","Johnson CA","Molina MM","Nagaraja-Grellscheid S","Georgiou M","Atkinson R","Ali R","Goertler F","Mozaffari-Jovin S","Davey T","Lako M"],"additional_accession":[]},"is_claimable":false,"name":"Activation of autophagy reverses progressive and deleterious protein aggregation in PRPF31 patient-induced pluripotent stem cell-derived retinal pigment epithelium cells.","description":"<h4>Introduction</h4>Mutations in pre-mRNA processing factor 31 (PRPF31), a core protein of the spliceosomal tri-snRNP complex, cause autosomal-dominant retinitis pigmentosa (adRP). It has remained an enigma why mutations in ubiquitously expressed tri-snRNP proteins result in retina-specific disorders, and so far, the underlying mechanism of splicing factors-related RP is poorly understood.<h4>Methods</h4>We used the induced pluripotent stem cell (iPSC) technology to generate retinal organoids and RPE models from four patients with severe and very severe PRPF31-adRP, unaffected individuals and a CRISPR/Cas9 isogenic control.<h4>Results</h4>To fully assess the impacts of PRPF31 mutations, quantitative proteomics analyses of retinal organoids and RPE cells were carried out showing RNA splici","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-04T23:33:46.31Z","creation":"2025-04-04T23:33:46.31Z"},"accession":"S-EPMC8926896","cross_references":{"pubmed":["35297555"],"doi":["10.1002/ctm2.759"]}}