RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23085988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23085988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23085988http://www.w3.org/2000/01/rdf-schema#comment"Sorting nexins (SNXs) are regulators of endosomal sorting. For the SNX-BAR subgroup, a Bin/Amphiphysin/Rvs (BAR) domain is vital for formation/stabilization of tubular subdomains that mediate cargo recycling. Here, by analysing the in vitro membrane remodelling properties of all 12 human SNX-BARs, we report that some, but not all, can elicit the formation of tubules with diameters that resemble sorting tubules observed in cells. We reveal that SNX-BARs display a restricted pattern of BAR domain-mediated dimerization, and by resolving a 2.8 Å structure of a SNX1-BAR domain homodimer, establish that dimerization is achieved in part through neutralization of charged residues in the hydrophobic BAR-dimerization interface. Membrane remodelling also requires functional amphipathic helices, predicted to be present in all SNX-BARs, and the formation of high order SNX-BAR oligomers through selective 'tip-loop' interactions. Overall, the restricted and selective nature of these interactions provide a molecular explanation for how distinct SNX-BAR-decorated tubules are nucleated from the same endosomal vacuole, as observed in living cells. Our data provide insight into the molecular mechanism that generates and organizes the tubular endosomal network."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2012.283"xsd:string
http://purl.uniprot.org/citations/23085988http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2012.283"xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Kloer D.P."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Kloer D.P."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Sessions R.B."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Sessions R.B."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Cullen P.J."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Cullen P.J."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Traer C.J."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Traer C.J."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Stamou D."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Stamou D."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"van Weering J.R."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"van Weering J.R."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Bhatia V.K."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/author"Bhatia V.K."xsd:string
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23085988http://purl.uniprot.org/core/date"2012"xsd:gYear