<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Vild CJ</submitter><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><pagination>10378-10386</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4036160</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>289(15)</volume><pubmed_abstract>The endosomal sorting complexes required for transport (ESCRT) are responsible for multivesicular body biogenesis, membrane abscission during cytokinesis, and retroviral budding. They function as transiently assembled molecular complexes on the membrane, and their disassembly requires the action of the AAA-ATPase Vps4. Vps4 is regulated by a multitude of ESCRT and ESCRT-related proteins. Binding of these proteins to Vps4 is often mediated via the microtubule-interacting and trafficking (MIT) domain of Vps4. Recently, a new Vps4-binding protein Vfa1 was identified in a yeast genetic screen, where overexpression of Vfa1 caused defects in vacuolar morphology. However, the function of Vfa1 and its role in vacuolar biology were largely unknown. Here, we provide the first detailed biochemical an</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity.</pubmed_title><pmcid>PMC4036160</pmcid><funding_grant_id>GM095769</funding_grant_id><funding_grant_id>R01 GM095769</funding_grant_id><pubmed_authors>Vild CJ</pubmed_authors><pubmed_authors>Xu Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity.</name><description>The endosomal sorting complexes required for transport (ESCRT) are responsible for multivesicular body biogenesis, membrane abscission during cytokinesis, and retroviral budding. They function as transiently assembled molecular complexes on the membrane, and their disassembly requires the action of the AAA-ATPase Vps4. Vps4 is regulated by a multitude of ESCRT and ESCRT-related proteins. Binding of these proteins to Vps4 is often mediated via the microtubule-interacting and trafficking (MIT) domain of Vps4. Recently, a new Vps4-binding protein Vfa1 was identified in a yeast genetic screen, where overexpression of Vfa1 caused defects in vacuolar morphology. However, the function of Vfa1 and its role in vacuolar biology were largely unknown. Here, we provide the first detailed biochemical an</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Apr</publication><modification>2025-04-19T01:12:07.353Z</modification><creation>2019-03-27T01:28:58Z</creation></dates><accession>S-EPMC4036160</accession><cross_references><pubmed>24567329</pubmed><doi>10.1074/jbc.M113.532960</doi><doi>10.1074/jbc.m113.532960</doi></cross_references></HashMap>