{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Ahmad I"],"funding":["NIAID NIH HHS"],"pubmed_abstract":["Serine incorporator 5 (SERINC5) is a host restriction factor that targets certain enveloped viruses, including human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MLV). It integrates into the viral envelope from the cell surface, inhibiting viral entry. SERINC5 is transported to the cell surface via polyubiquitination, while a single K130R mutation retains it in the cytoplasm. Both HIV-1 Nef and MLV glycoGag proteins antagonize SERINC5 by reducing its expression in producer cells. Here, we report that MLV glycoGag employs selective autophagy to downregulate SERINC5, demonstrating a more potent mechanism for decreasing its cell surface expression. Although glycoGag is a type II integral membrane protein, it primarily localizes to the cytoplasm and undergoes rapid proteaso"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.03.06.641798"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11908239"],"repository":["biostudies-literature"],"pubmed_title":["Murine Leukemia Virus GlycoGag Antagonizes SERINC5 via ER-phagy Receptor RETREG1."],"pmcid":["PMC11908239"],"funding_grant_id":["R01 AI145504"],"pubmed_authors":["Liu X","Khan I","Li LF","Li S","Zhang J","Zheng YH","Ahmad I","Li R","Su W","Wu Y","Liu W"],"additional_accession":[]},"is_claimable":false,"name":"Murine Leukemia Virus GlycoGag Antagonizes SERINC5 via ER-phagy Receptor RETREG1.","description":"Serine incorporator 5 (SERINC5) is a host restriction factor that targets certain enveloped viruses, including human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MLV). It integrates into the viral envelope from the cell surface, inhibiting viral entry. SERINC5 is transported to the cell surface via polyubiquitination, while a single K130R mutation retains it in the cytoplasm. Both HIV-1 Nef and MLV glycoGag proteins antagonize SERINC5 by reducing its expression in producer cells. Here, we report that MLV glycoGag employs selective autophagy to downregulate SERINC5, demonstrating a more potent mechanism for decreasing its cell surface expression. Although glycoGag is a type II integral membrane protein, it primarily localizes to the cytoplasm and undergoes rapid proteaso","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-05-19T03:08:25.985Z","creation":"2025-04-04T03:04:06.721Z"},"accession":"S-EPMC11908239","cross_references":{"pubmed":["40093084"],"doi":["10.1101/2025.03.06.641798"]}}