{"entity": "researcher", "timestamp": "2026-08-20T20:40:34.777Z", "family": "Masucci", "given": "Maria G", "initials": "MG", "orcid": "0000-0002-5541-2809", "affiliations": ["Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ac1411f252f403485d658f2c74204f0.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ac1411f252f403485d658f2c74204f0"}}, "publications": [{"entity": "publication", "iuid": "c4b9cca27860453e84b806a7987f215d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c4b9cca27860453e84b806a7987f215d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c4b9cca27860453e84b806a7987f215d"}}, "title": "The Epstein-Barr virus deubiquitinase BPLF1 regulates stress-induced ribosome UFMylation and reticulophagy.", "authors": [{"family": "Liu", "given": "Jiangnan", "initials": "J", "orcid": "0000-0002-3086-7567", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5c28ada139d64dca82657d1ee5f1d2b0.json"}}, {"family": "Nagy", "given": "Noemi", "initials": "N", "orcid": "0000-0002-7800-3493", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3f27465b7465457c89f55ef01194da02.json"}}, {"family": "Ayala-Torres", "given": "Carlos", "initials": "C", "orcid": "0000-0002-2306-6788", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/789af2aa7d6543a9bdb157d59dceb458.json"}}, {"family": "Bleuse", "given": "Solenne", "initials": "S"}, {"family": "Aguilar-Alonso", "given": "Francisco", "initials": "F", "orcid": "0000-0003-4457-5642", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bf76e002fbd046b1840cc6988e559ea8.json"}}, {"family": "Larsson", "given": "Ola", "initials": "O", "orcid": "0000-0003-1412-1308", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3f81c6cbbe564d38bc78d1af5153d804.json"}}, {"family": "Masucci", "given": "Maria G", "initials": "MG", "orcid": "0000-0002-5541-2809", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ac1411f252f403485d658f2c74204f0.json"}}], "type": "journal article", "published": "2025-05-00", "journal": {"title": "Autophagy", "issn": "1554-8635", "volume": "21", "issue": "5", "pages": "996-1018", "issn-l": "1554-8627"}, "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 UFMylation of the ER membrane protein CYB5R3 by the UFL1 ligase. Instead, it copurified with ribosomes in sucrose gradients and abrogated a ZNF598- and LTN1-independent ubiquitination event required for RPL26 UFMylation. Physiological levels of BPLF1 impaired the UFMylation of RPL26 in productively EBV-infected cells, pointing to an important role of the enzyme in regulating the translation quality control that allows the efficient synthesis of viral proteins and the production of infectious virus.Abbreviation: BPLF1, BamH1 P fragment left open readingframe-1; CDK5RAP3, CDK5regulatory subunit associated protein 3; ChFP, mCherry fluorescent protein; DDRGK1, DDRGKdomain containing 1; EBV, Epstein-Barr virus; eGFP, enhancedGFP; ER-RQC, endoplasmicreticulum-associated ribosome quality control; LCL, EBV-carryinglymphoblastoid cell line; GFP, green fluorescent protein; RQC, ribosome quality control; SRP, signal recognition particle; UFM1, ubiquitin fold modifier 1; UFL1, UFM1 specific ligase 1.", "doi": "10.1080/15548627.2024.2440846", "pmid": "39842454", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12013442"}], "notes": [], "created": "2026-08-20T09:37:01.535Z", "modified": "2026-08-20T09:37:01.762Z"}, {"entity": "publication", "iuid": "e00b7b7acc294b5fb8c84f0631bba0b9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e00b7b7acc294b5fb8c84f0631bba0b9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e00b7b7acc294b5fb8c84f0631bba0b9"}}, "title": "14-3-3 scaffold proteins mediate the inactivation of trim25 and inhibition of the type I interferon response by herpesvirus deconjugases.", "authors": [{"family": "Gupta", "given": "Soham", "initials": "S", "orcid": "0000-0003-1136-3010", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1d5cddb6da03462189049a2ca72f0e66.json"}}, {"family": "Yl\u00e4-Anttila", "given": "P\u00e4ivi", "initials": "P", "orcid": "0000-0002-5794-5094", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/60ff8f7881314618a9d400699d5e329f.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A"}, {"family": "Masucci", "given": "Maria G", "initials": "MG", "orcid": "0000-0002-5541-2809", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ac1411f252f403485d658f2c74204f0.json"}}], "type": "journal article", "published": "2019-11-00", "journal": {"title": "PLoS Pathog", "issn": "1553-7374", "volume": "15", "issue": "11", "pages": "e1008146", "issn-l": "1553-7366"}, "abstract": "The 14-3-3 molecular scaffolds promote type I interferon (IFN) responses by stabilizing the interaction of RIG-I with the TRIM25 ligase. Viruses have evolved unique strategies to halt this cellular response to support their replication and spread. Here, we report that the ubiquitin deconjugase (DUB) encoded in the N-terminus of the Epstein-Barr virus (EBV) large tegument protein BPLF1 harnesses 14-3-3 molecules to promote TRIM25 autoubiquitination and sequestration of the ligase into inactive protein aggregates. Catalytically inactive BPLF1 induced K48-linked autoubiquitination and degradation of TRIM25 while the ligase was mono- or di-ubiquitinated in the presence of the active viral enzyme and formed cytosolic aggregates decorated by the autophagy receptor p62/SQSTM1. Aggregate formation and the inhibition of IFN response were abolished by mutations of solvent exposed residues in helix-2 of BPLF1 that prevented binding to 14-3-3 while preserving both catalytic activity and binding to TRIM25. 14-3-3 interacted with the Coiled-Coil (CC) domain of TRIM25 in in vitro pulldown, while BPLF1 interacted with both the CC and B-box domains, suggesting that 14-3-3 positions BPLF1 at the ends of the CC dimer, close to known autoubiquitination sites. Our findings provide a molecular understanding of the mechanism by which a viral deubiquitinase inhibits the IFN response and emphasize the role of 14-3-3 proteins in modulating antiviral defenses.", "doi": "10.1371/journal.ppat.1008146", "pmid": "31710640", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6874091"}, {"db": "pii", "key": "PPATHOGENS-D-19-01153"}], "notes": [], "created": "2026-08-20T12:44:41.459Z", "modified": "2026-08-20T12:44:41.524Z"}]}