{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Klossel S"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","European Research Council","Deutsche Forschungsgemeinschaft"],"pagination":["1870-1897"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11066047"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(9)"],"pubmed_abstract":["Yeast vacuoles perform crucial cellular functions as acidic degradative organelles, storage compartments, and signaling hubs. These functions are mediated by important protein complexes, including the vacuolar-type H<sup>+</sup>-ATPase (V-ATPase), responsible for organelle acidification. To gain a more detailed understanding of vacuole function, we performed cross-linking mass spectrometry on isolated vacuoles, detecting many known as well as novel protein-protein interactions. Among these, we identified the uncharacterized TLDc-domain-containing protein Rtc5 as a novel interactor of the V-ATPase. We further analyzed the influence of Rtc5 and of Oxr1, the only other yeast TLDc-domain-containing protein, on V-ATPase function. We find that both Rtc5 and Oxr1 promote the disassembly of the va"],"journal":["The EMBO journal"],"pubmed_title":["Yeast TLDc domain proteins regulate assembly state and subcellular localization of the V-ATPase."],"pmcid":["PMC11066047"],"funding_grant_id":["LI 3260/5-1","GO 3313/1-1","STG 949184","949184"],"pubmed_authors":["Zhu Y","Amado L","Klossel S","Gonzalez Montoro A","Bisinski DD","Ruta J","Liu F"],"additional_accession":[]},"is_claimable":false,"name":"Yeast TLDc domain proteins regulate assembly state and subcellular localization of the V-ATPase.","description":"Yeast vacuoles perform crucial cellular functions as acidic degradative organelles, storage compartments, and signaling hubs. These functions are mediated by important protein complexes, including the vacuolar-type H<sup>+</sup>-ATPase (V-ATPase), responsible for organelle acidification. To gain a more detailed understanding of vacuole function, we performed cross-linking mass spectrometry on isolated vacuoles, detecting many known as well as novel protein-protein interactions. Among these, we identified the uncharacterized TLDc-domain-containing protein Rtc5 as a novel interactor of the V-ATPase. We further analyzed the influence of Rtc5 and of Oxr1, the only other yeast TLDc-domain-containing protein, on V-ATPase function. We find that both Rtc5 and Oxr1 promote the disassembly of the va","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T07:02:03.675Z","creation":"2026-04-15T03:15:35.659Z"},"accession":"S-EPMC11066047","cross_references":{"pubmed":["38589611"],"doi":["10.1038/s44318-024-00097-2"]}}