{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Oresic K"],"funding":["NIAID NIH HHS"],"pagination":["5905-14"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2645836"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["284(9)"],"pubmed_abstract":["The human cytomegalovirus proteins US2 and US11 have co-opted endoplasmic reticulum (ER) quality control to facilitate the destruction of major histocompatibility complex class I heavy chains. The class I heavy chains are dislocated from the ER to the cytosol, where they are deglycosylated and subsequently degraded by the proteasome. We examined the role of TRAM1 (translocating chain-associated membrane protein-1) in the dislocation of class I molecules using US2- and US11-expressing cells. TRAM1 is an ER protein initially characterized for its role in processing nascent polypeptides. Co-immunoprecipitation studies demonstrated that TRAM1 can complex with the wild type US2 and US11 proteins as well as deglycosylated and polyubiquitinated class I degradation intermediates. In studies using "],"journal":["The Journal of biological chemistry"],"pubmed_title":["TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein."],"pmcid":["PMC2645836"],"funding_grant_id":["U19 AI062623","AI060905"],"pubmed_authors":["Tortorella D","Oresic K","Ng CL"],"additional_accession":[]},"is_claimable":false,"name":"TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein.","description":"The human cytomegalovirus proteins US2 and US11 have co-opted endoplasmic reticulum (ER) quality control to facilitate the destruction of major histocompatibility complex class I heavy chains. The class I heavy chains are dislocated from the ER to the cytosol, where they are deglycosylated and subsequently degraded by the proteasome. We examined the role of TRAM1 (translocating chain-associated membrane protein-1) in the dislocation of class I molecules using US2- and US11-expressing cells. TRAM1 is an ER protein initially characterized for its role in processing nascent polypeptides. Co-immunoprecipitation studies demonstrated that TRAM1 can complex with the wild type US2 and US11 proteins as well as deglycosylated and polyubiquitinated class I degradation intermediates. In studies using ","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Feb","modification":"2025-04-04T07:58:19.195Z","creation":"2019-03-27T00:20:49Z"},"accession":"S-EPMC2645836","cross_references":{"pubmed":["19121997"],"doi":["10.1074/jbc.m807568200","10.1074/jbc.M807568200"]}}