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http://purl.uniprot.org/citations/32651375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32651375http://www.w3.org/2000/01/rdf-schema#comment"DOCK (dedicator of cytokinesis) proteins are multidomain guanine nucleotide exchange factors (GEFs) for RHO GTPases that regulate intracellular actin dynamics. DOCK proteins share catalytic (DOCKDHR2) and membrane-associated (DOCKDHR1) domains. The structurally-related DOCK1 and DOCK2 GEFs are specific for RAC, and require ELMO (engulfment and cell motility) proteins for function. The N-terminal RAS-binding domain (RBD) of ELMO (ELMORBD) interacts with RHOG to modulate DOCK1/2 activity. Here, we determine the cryo-EM structures of DOCK2-ELMO1 alone, and as a ternary complex with RAC1, together with the crystal structure of a RHOG-ELMO2RBD complex. The binary DOCK2-ELMO1 complex adopts a closed, auto-inhibited conformation. Relief of auto-inhibition to an active, open state, due to a conformational change of the ELMO1 subunit, exposes binding sites for RAC1 on DOCK2DHR2, and RHOG and BAI GPCRs on ELMO1. Our structure explains how up-stream effectors, including DOCK2 and ELMO1 phosphorylation, destabilise the auto-inhibited state to promote an active GEF."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.org/dc/terms/identifier"doi:10.1038/s41467-020-17271-9"xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Barford D."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Chang L."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"McLaughlin S.H."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Yang J."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Smith M.J."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Boland A."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Cote J.F."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Jo C.H."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Abu-Thuraia A."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/author"Killoran R.C."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/pages"3464"xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/title"Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state."xsd:string
http://purl.uniprot.org/citations/32651375http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/32651375http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32651375
http://purl.uniprot.org/citations/32651375http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32651375
http://purl.uniprot.org/uniprot/#_A4D1X5-mappedCitation-32651375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32651375
http://purl.uniprot.org/uniprot/#_A0A2X0SFD3-mappedCitation-32651375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32651375
http://purl.uniprot.org/uniprot/#_B3KXW9-mappedCitation-32651375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32651375
http://purl.uniprot.org/uniprot/#_B3KY14-mappedCitation-32651375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32651375