{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":48,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["30(11)"],"submitter":["Ren X"],"funding":["Intramural NIH HHS"],"pubmed_abstract":["The ESCRT-0 and ESCRT-I complexes coordinate the clustering of ubiquitinated cargo with intralumenal budding of the endosomal membrane, two essential steps in vacuolar/lysosomal protein sorting from yeast to humans. The 1.85-Å crystal structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 centred on Trp16. This novel site is completely different from the C-terminal part of the human UEV domain that binds to P(S/T)AP motifs of human ESCRT-0 and HIV-1 Gag. Disruption of the novel PSDP-binding site eliminates the interaction in vitro and blocks enrichment of Vps23 in endosome-related class E compartments in yeast cells. However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms."],"journal":["The EMBO journal"],"pagination":["2130-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3117643"],"repository":["biostudies-literature"],"pubmed_title":["Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast."],"pmcid":["PMC3117643"],"pubmed_authors":["Ren X","Hurley JH"],"view_count":["48"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for endosomal recruitment of ESCRT-I by ESCRT-0 in yeast.","description":"The ESCRT-0 and ESCRT-I complexes coordinate the clustering of ubiquitinated cargo with intralumenal budding of the endosomal membrane, two essential steps in vacuolar/lysosomal protein sorting from yeast to humans. The 1.85-Å crystal structure of interacting regions of the yeast ESCRT-0 and ESCRT-I complexes reveals that PSDP motifs of the Vps27 ESCRT-0 subunit bind to a novel electropositive N-terminal site on the UEV domain of the ESCRT-I subunit Vps23 centred on Trp16. This novel site is completely different from the C-terminal part of the human UEV domain that binds to P(S/T)AP motifs of human ESCRT-0 and HIV-1 Gag. Disruption of the novel PSDP-binding site eliminates the interaction in vitro and blocks enrichment of Vps23 in endosome-related class E compartments in yeast cells. However, this site is non-essential for sorting of the ESCRT cargo Cps1. Taken together, these results show how a conserved motif/domain pair can evolve to use strikingly different binding modes in different organisms.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2024-11-20T04:58:22.984Z","creation":"2019-03-27T00:42:43Z"},"accession":"S-EPMC3117643","cross_references":{"pubmed":["21505419"],"doi":["10.1038/emboj.2011.122"]}}