{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kliza KW"],"funding":["The Francis Crick Institute","Medical Research Council","Wellcome Trust"],"pagination":["183"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11032371"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Signalling through TNFR1 modulates proinflammatory gene transcription and programmed cell death, and its impairment causes autoimmune diseases and cancer. NEDD4-binding protein 1 (N4BP1) is a critical suppressor of proinflammatory cytokine production that acts as a regulator of innate immune signalling and inflammation. However, our current understanding about the molecular properties that enable N4BP1 to exert its suppressive potential remain limited. Here, we show that N4BP1 is a novel linear ubiquitin reader that negatively regulates NFκB signalling by its unique dimerization-dependent ubiquitin-binding module that we named LUBIN. Dimeric N4BP1 strategically positions two non-selective ubiquitin-binding domains to ensure preferential recognition of linear ubiquitin. Under proinflammator"],"journal":["Cell death discovery"],"pubmed_title":["N4BP1 functions as a dimerization-dependent linear ubiquitin reader which regulates TNF signalling."],"pmcid":["PMC11032371"],"funding_grant_id":["FC001029","CC1068","CC1078","MR/X036944/1"],"pubmed_authors":["Kuntin D","Kliza KW","Hofmann K","Schaubeck S","Garnett JA","Husnjak K","Kunzelmann S","Fornili A","Song W","Pinzuti I","Pandini A","Stieglitz B"],"additional_accession":[]},"is_claimable":false,"name":"N4BP1 functions as a dimerization-dependent linear ubiquitin reader which regulates TNF signalling.","description":"Signalling through TNFR1 modulates proinflammatory gene transcription and programmed cell death, and its impairment causes autoimmune diseases and cancer. NEDD4-binding protein 1 (N4BP1) is a critical suppressor of proinflammatory cytokine production that acts as a regulator of innate immune signalling and inflammation. However, our current understanding about the molecular properties that enable N4BP1 to exert its suppressive potential remain limited. Here, we show that N4BP1 is a novel linear ubiquitin reader that negatively regulates NFκB signalling by its unique dimerization-dependent ubiquitin-binding module that we named LUBIN. Dimeric N4BP1 strategically positions two non-selective ubiquitin-binding domains to ensure preferential recognition of linear ubiquitin. Under proinflammator","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-02T11:24:26.444Z","creation":"2026-05-27T03:07:24.645Z"},"accession":"S-EPMC11032371","cross_references":{"pubmed":["38643192"],"doi":["10.1038/s41420-024-01913-8"]}}