{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Williams JM"],"funding":["NIAID NIH HHS","PHS HHS"],"pagination":["785-95"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3596249"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(6)"],"pubmed_abstract":["Cholera toxin (CT) traffics from the host cell surface to the endoplasmic reticulum (ER), where the toxin's catalytic CTA1 subunit retrotranslocates to the cytosol to induce toxicity. In the ER, CT is captured by the E3 ubiquitin ligase Hrd1 via an undefined mechanism to prepare for retrotranslocation. Using loss-of-function and gain-of-function approaches, we demonstrate that the ER-resident factor ERdj5 promotes CTA1 retrotranslocation, in part, via its J domain. This Hsp70 cochaperone regulates binding between CTA and the ER Hsp70 BiP, a chaperone previously implicated in toxin retrotranslocation. Importantly, ERdj5 interacts with the Hrd1 adaptor Sel1L directly through Sel1L's N-terminal lumenal domain, thereby linking ERdj5 to the Hrd1 complex. Sel1L itself also binds CTA and facilita"],"journal":["Molecular biology of the cell"],"pubmed_title":["The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation."],"pmcid":["PMC3596249"],"funding_grant_id":["R01 083252-04","R01 AI083252"],"pubmed_authors":["Inoue T","Tsai B","Banks L","Williams JM"],"additional_accession":[]},"is_claimable":false,"name":"The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation.","description":"Cholera toxin (CT) traffics from the host cell surface to the endoplasmic reticulum (ER), where the toxin's catalytic CTA1 subunit retrotranslocates to the cytosol to induce toxicity. In the ER, CT is captured by the E3 ubiquitin ligase Hrd1 via an undefined mechanism to prepare for retrotranslocation. Using loss-of-function and gain-of-function approaches, we demonstrate that the ER-resident factor ERdj5 promotes CTA1 retrotranslocation, in part, via its J domain. This Hsp70 cochaperone regulates binding between CTA and the ER Hsp70 BiP, a chaperone previously implicated in toxin retrotranslocation. Importantly, ERdj5 interacts with the Hrd1 adaptor Sel1L directly through Sel1L's N-terminal lumenal domain, thereby linking ERdj5 to the Hrd1 complex. Sel1L itself also binds CTA and facilita","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Mar","modification":"2025-04-04T14:33:26.824Z","creation":"2019-03-27T01:06:02Z"},"accession":"S-EPMC3596249","cross_references":{"pubmed":["23363602"],"doi":["10.1091/mbc.E12-07-0522"]}}