{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yifrach E"],"funding":["The Ariane de Rothschild Women Doctoral Program","Blythe Brenden-Mann foundation","European Research Council","ERC CoG","Kekst Family Institute for Medical Genetics","Israeli Science Foundation (ISF)"],"pagination":["e11186"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9513677"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(9)"],"pubmed_abstract":["Seventy years following the discovery of peroxisomes, their complete proteome, the peroxi-ome, remains undefined. Uncovering the peroxi-ome is crucial for understanding peroxisomal activities and cellular metabolism. We used high-content microscopy to uncover peroxisomal proteins in the model eukaryote - Saccharomyces cerevisiae. This strategy enabled us to expand the known peroxi-ome by ~40% and paved the way for performing systematic, whole-organellar proteome assays. By characterizing the sub-organellar localization and protein targeting dependencies into the organelle, we unveiled non-canonical targeting routes. Metabolomic analysis of the peroxi-ome revealed the role of several newly identified resident enzymes. Importantly, we found a regulatory role of peroxisomes during gluconeogen"],"journal":["Molecular systems biology"],"pubmed_title":["Systematic multi-level analysis of an organelle proteome reveals new peroxisomal functions."],"pmcid":["PMC9513677"],"funding_grant_id":["ISF914/22","864068"],"pubmed_authors":["Yifrach E","Weill U","Waterham HR","Holbrook-Smith D","Visser W","Tirosh A","Wanders RJA","Bibi C","Wilmanns M","Schuldiner M","Erdmann R","Othman A","Galor S","Zamboni N","Burgi J","Eisenstein M","Zalckvar E","Rudowitz M","van Roermund CW","Fadel A","Peleg Y"],"additional_accession":[]},"is_claimable":false,"name":"Systematic multi-level analysis of an organelle proteome reveals new peroxisomal functions.","description":"Seventy years following the discovery of peroxisomes, their complete proteome, the peroxi-ome, remains undefined. Uncovering the peroxi-ome is crucial for understanding peroxisomal activities and cellular metabolism. We used high-content microscopy to uncover peroxisomal proteins in the model eukaryote - Saccharomyces cerevisiae. This strategy enabled us to expand the known peroxi-ome by ~40% and paved the way for performing systematic, whole-organellar proteome assays. By characterizing the sub-organellar localization and protein targeting dependencies into the organelle, we unveiled non-canonical targeting routes. Metabolomic analysis of the peroxi-ome revealed the role of several newly identified resident enzymes. Importantly, we found a regulatory role of peroxisomes during gluconeogen","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-04-19T17:38:14.231Z","creation":"2025-04-19T17:38:14.231Z"},"accession":"S-EPMC9513677","cross_references":{"pubmed":["36164978"],"doi":["10.15252/msb.202211186"]}}