{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["105(4)"],"submitter":["Hunter LM"],"funding":["Medical Research Council","NIHR Cambridge Biomedical Research Centre","National Institute for Health Research (NIHR)","Wellcome Trust"],"pubmed_abstract":["The human cytomegalovirus (HCMV) pUS2 glycoprotein exploits the host's endoplasmic reticulum (ER)-associated degradation (ERAD) pathway to degrade major histocompatibility complex class I (MHC-I) and prevent antigen presentation. Beyond MHC-I, pUS2 has been shown to target a range of cellular proteins for degradation, preventing their cell surface expression. Here we have identified a novel pUS2 target, ER-resident protein lectin mannose binding 2 like (LMAN2L). pUS2 expression was both necessary and sufficient for the downregulation of LMAN2L, which was dependent on the cellular E3 ligase TRC8. Given the hypothesized role of LMAN2L in the trafficking of glycoproteins, we employed proteomic plasma membrane profiling to measure LMAN2L-dependent changes at the cell surface. A known pUS2 targ"],"journal":["The Journal of general virology"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11083459"],"repository":["biostudies-literature"],"pubmed_title":["HCMV US2 co-opts TRC8 to degrade the endoplasmic reticulum-resident protein LMAN2L."],"pmcid":["PMC11083459"],"funding_grant_id":["108070/Z/15/Z","NIHR203312","MR/S00971X/1","226615/Z/22/Z","226615","108070","220015/Z/19/Z","220015"],"pubmed_authors":["Kite J","Nightingale K","Stanton RJ","Fielding CA","Weekes MP","Hunter LM","Nobre L","Fletcher-Etherington A","Antrobus R"],"additional_accession":[]},"is_claimable":false,"name":"HCMV US2 co-opts TRC8 to degrade the endoplasmic reticulum-resident protein LMAN2L.","description":"The human cytomegalovirus (HCMV) pUS2 glycoprotein exploits the host's endoplasmic reticulum (ER)-associated degradation (ERAD) pathway to degrade major histocompatibility complex class I (MHC-I) and prevent antigen presentation. Beyond MHC-I, pUS2 has been shown to target a range of cellular proteins for degradation, preventing their cell surface expression. Here we have identified a novel pUS2 target, ER-resident protein lectin mannose binding 2 like (LMAN2L). pUS2 expression was both necessary and sufficient for the downregulation of LMAN2L, which was dependent on the cellular E3 ligase TRC8. Given the hypothesized role of LMAN2L in the trafficking of glycoproteins, we employed proteomic plasma membrane profiling to measure LMAN2L-dependent changes at the cell surface. A known pUS2 targ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-05-29T03:11:28.393Z","creation":"2026-05-29T03:06:15.405Z"},"accession":"S-EPMC11083459","cross_references":{"pubmed":["38687323"],"doi":["10.1099/jgv.0.001980"]}}