{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Boutouja F"],"funding":["Deutsche Forschungsgemeinschaft","Konrad-Adenauer-Stiftung"],"pagination":["10557"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6646403"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["The vacuole is the hydrolytic compartment of yeast cells and has a similar function as the lysosome of higher eukaryotes in detoxification and recycling of macromolecules. We analysed the contribution of single vacuolar enzymes to pexophagy and identified the phospholipase Atg15, the V-ATPase factor Vma2 and the serine-protease Prb1 along with the already known aspartyl-protease Pep4 (Proteinase A) to be required for this pathway. We also analysed the trafficking receptor Vps10, which is required for an efficient vacuolar targeting of the precursor form of Pep4. Here we demonstrate a novel context-dependent role of Vps10 in autophagy. We show that reduced maturation of Pep4 in a VPS10-deletion strain affects the proteolytic activity of the vacuole depending on the type and amount of substr"],"journal":["Scientific reports"],"pubmed_title":["Vps10-mediated targeting of Pep4 determines the activity of the vacuole in a substrate-dependent manner."],"pmcid":["PMC6646403"],"funding_grant_id":["FOR1905","SFB642"],"pubmed_authors":["Stiehm CM","El Magraoui F","Mastalski T","Brinkmeier R","Boutouja F","Platta HW","Reidick C"],"additional_accession":[]},"is_claimable":false,"name":"Vps10-mediated targeting of Pep4 determines the activity of the vacuole in a substrate-dependent manner.","description":"The vacuole is the hydrolytic compartment of yeast cells and has a similar function as the lysosome of higher eukaryotes in detoxification and recycling of macromolecules. We analysed the contribution of single vacuolar enzymes to pexophagy and identified the phospholipase Atg15, the V-ATPase factor Vma2 and the serine-protease Prb1 along with the already known aspartyl-protease Pep4 (Proteinase A) to be required for this pathway. We also analysed the trafficking receptor Vps10, which is required for an efficient vacuolar targeting of the precursor form of Pep4. Here we demonstrate a novel context-dependent role of Vps10 in autophagy. We show that reduced maturation of Pep4 in a VPS10-deletion strain affects the proteolytic activity of the vacuole depending on the type and amount of substr","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jul","modification":"2025-04-27T04:16:01.718Z","creation":"2019-08-02T07:01:41Z"},"accession":"S-EPMC6646403","cross_references":{"pubmed":["31332264"],"doi":["10.1038/s41598-019-47184-7"]}}