{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["21(5)"],"submitter":["Liu J"],"funding":["the Swedish Cancer Foundation","Swedish Research Council","the Karolinska Institutet"],"pubmed_abstract":["The synthesis of membrane and secreted proteins is safeguarded by an endoplasmic reticulum-associated ribosome quality control (ER-RQC) that promotes the disposal of defective translation products by the proteasome or via a lysosome-dependent pathway involving the degradation of portions of the ER by macroautophagy (reticulophagy). The UFMylation of RPL26 on ER-stalled ribosomes is essential for activating the ER-RQC and reticulophagy. Here, we report that the viral deubiquitinase (vDUB) encoded in the N-terminal domain of the Epstein-Barr virus (EBV) large tegument protein BPLF1 hinders the UFMylation of RPL26 on ribosomes that stall at the ER, promotes the stabilization of ER-RQC substrates, and inhibits reticulophagy. The vDUB did not act as a de-UFMylase or interfere with the UFMylatio"],"journal":["Autophagy"],"pagination":["996-1018"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12013442"],"repository":["biostudies-literature"],"pubmed_title":["The Epstein-Barr virus deubiquitinase BPLF1 regulates stress-induced ribosome UFMylation and reticulophagy."],"pmcid":["PMC12013442"],"pubmed_authors":["Bleuse S","Liu J","Nagy N","Ayala-Torres C","Larsson O","Aguilar-Alonso F","Masucci MG"],"additional_accession":[]},"is_claimable":false,"name":"The Epstein-Barr virus deubiquitinase BPLF1 regulates stress-induced ribosome UFMylation and reticulophagy.","description":"The synthesis of membrane and secreted proteins is safeguarded by an endoplasmic reticulum-associated ribosome quality control (ER-RQC) that promotes the disposal of defective translation products by the proteasome or via a lysosome-dependent pathway involving the degradation of portions of the ER by macroautophagy (reticulophagy). The UFMylation of RPL26 on ER-stalled ribosomes is essential for activating the ER-RQC and reticulophagy. Here, we report that the viral deubiquitinase (vDUB) encoded in the N-terminal domain of the Epstein-Barr virus (EBV) large tegument protein BPLF1 hinders the UFMylation of RPL26 on ribosomes that stall at the ER, promotes the stabilization of ER-RQC substrates, and inhibits reticulophagy. The vDUB did not act as a de-UFMylase or interfere with the UFMylatio","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-07-15T11:03:23.58Z","creation":"2025-07-07T03:10:05.705Z"},"accession":"S-EPMC12013442","cross_references":{"pubmed":["39842454"],"doi":["10.1080/15548627.2024.2440846"]}}