RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23105107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23105107http://www.w3.org/2000/01/rdf-schema#comment"The AAA-ATPase Vps4 is critical for function of the multivesicular body sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear. The fragment Vps60(128-186) was reported to display the full activity of Vps60. Vta1 interacts with Vps60 using its N-terminal domain (Vta1NTD). In this work, the structure of Vps60(128-186) in complex with Vta1NTD was determined using NMR techniques, demonstrating a novel recognition mode of the microtubule-interacting and transport (MIT) domain in which Vps60(128-186) interacts with Vta1NTD through helices α4' and α5', extending over Vta1NTD MIT2 domain helices 1-3. The Vps60 binding does not result in Vta1 conformational changes, further revealing the fact that Vps4 ATPase is enhanced by the interaction between Vta1 and Vps60 in an unanticipated manner."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.390724"xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Cao C."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Gong F."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Ju J."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Liu M."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Shen J."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Zhao B."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Yang Z."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Xu Z."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Lan W."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/author"Vild C."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/pages"43899-43908"xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/title"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway."xsd:string
http://purl.uniprot.org/citations/23105107http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/23105107http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23105107
http://purl.uniprot.org/citations/23105107http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23105107
http://purl.uniprot.org/uniprot/#_A0A8H4BX99-mappedCitation-23105107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23105107
http://purl.uniprot.org/uniprot/#_A0A6A5Q4G9-mappedCitation-23105107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23105107
http://purl.uniprot.org/uniprot/#_Q06263-mappedCitation-23105107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23105107