<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Oresic K</submitter><funding>NIAID NIH HHS</funding><pagination>5905-14</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2645836</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>284(9)</volume><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 </pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein.</pubmed_title><pmcid>PMC2645836</pmcid><funding_grant_id>U19 AI062623</funding_grant_id><funding_grant_id>AI060905</funding_grant_id><pubmed_authors>Tortorella D</pubmed_authors><pubmed_authors>Oresic K</pubmed_authors><pubmed_authors>Ng CL</pubmed_authors></additional><is_claimable>false</is_claimable><name>TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein.</name><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 </description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 Feb</publication><modification>2025-04-04T07:58:19.195Z</modification><creation>2019-03-27T00:20:49Z</creation></dates><accession>S-EPMC2645836</accession><cross_references><pubmed>19121997</pubmed><doi>10.1074/jbc.m807568200</doi><doi>10.1074/jbc.M807568200</doi></cross_references></HashMap>