{"entity": "researcher", "timestamp": "2026-10-01T11:58:32.420Z", "family": "Cohen", "given": "Michael S", "initials": "MS", "orcid": "0000-0002-7636-4156", "affiliations": ["Department of Chemical Physiology and Biochemistry, Oregon Health and Science University, Portland, OR, USA."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/00f8af9cc9284322845ae12ddc5718f3.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/00f8af9cc9284322845ae12ddc5718f3"}}, "publications": [{"entity": "publication", "iuid": "ecaff23e000f441da9de3284e425ea40", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/ecaff23e000f441da9de3284e425ea40.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/ecaff23e000f441da9de3284e425ea40"}}, "title": "Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15.", "authors": [{"family": "Ebenwaldner", "given": "Carmen", "initials": "C", "orcid": "0000-0002-7919-2994", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/7b201a3bab5844f09a7d7e7c21c2b73e.json"}}, {"family": "Garc\u00eda Saura", "given": "Antonio Gin\u00e9s", "initials": "AG"}, {"family": "Ekstr\u00f6m", "given": "Simon", "initials": "S", "orcid": "0000-0002-7694-285X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/277129edad3b4b77b645be7353cec439.json"}}, {"family": "Bernfur", "given": "Katja", "initials": "K", "orcid": "0000-0002-7927-9563", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9de098f285774da583545f697f7032cf.json"}}, {"family": "Moche", "given": "Martin", "initials": "M"}, {"family": "Logan", "given": "Derek T", "initials": "DT", "orcid": "0000-0002-0098-8560", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/64e6e27f8c8f470e9b390575d3bdbf17.json"}}, {"family": "Cohen", "given": "Michael S", "initials": "MS", "orcid": "0000-0002-7636-4156", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/00f8af9cc9284322845ae12ddc5718f3.json"}}, {"family": "Sch\u00fcler", "given": "Herwig", "initials": "H", "orcid": "0000-0003-4059-3501", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a66d04210ea41c2bbb0a5ee187c7b76.json"}}], "type": "journal article", "published": "2025-10-29", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "16", "issue": "1", "pages": "9567", "issn-l": "2041-1723"}, "abstract": "PARP15 is a mono-ADP-ribosyltransferase that targets an unknown set of proteins as well as RNA. Its evolutionary relationship with PARP14 suggests roles in antiviral defence; its localization to stress granules points to functions in the regulation of translation. Here we show that the transferase domain of PARP15 dimerizes in solution; the formation of dimers is a prerequisite for catalytic activity and monomeric mutant variants of the domain are inactive. In cells, dimer-disrupting mutations abrogate catalytic activity and alter the subcellular localization of the full-length protein. Using biophysical methods, including X-ray crystallography and HDX-MS, we provide evidence for a regulatory mechanism by which dimerization enables correct target engagement rather than NAD+ co-substrate binding, and by which the two protomers of the dimer operate independently of one another. Together, our results uncover a regulatory mechanism in a PARP family enzyme.", "doi": "10.1038/s41467-025-65315-9", "pmid": "41162413", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12572374"}, {"db": "pii", "key": "10.1038/s41467-025-65315-9"}], "notes": [], "created": "2026-10-01T08:30:34.937Z", "modified": "2026-10-01T08:30:35.097Z"}]}