{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["28(11)"],"submitter":["Gupta D"],"pubmed_abstract":["LisH-domain-containing proteins are involved in diverse cellular processes and disease mechanisms, yet their functional interaction landscape remains poorly characterized. Here, we employed a proteomics-based strategy to systematically map the interaction network of 27 LisH-domain-containing proteins, uncovering 1,410 high-confidence interactions-90% of which are previously unreported. This network reveals unanticipated roles for LisH proteins in cellular regulation and uncovers links to human disease, including cancer-associated interactions. Focusing on Lis1, a cytoplasmic dynein regulator, we identify the RBR-E3 ubiquitin ligase ARIH2 as a key functional interactor. We show that Lis1 promotes ARIH2 deneddylation via the COP9 signalosome (CSN), modulating its ubiquitin ligase activity. A"],"journal":["iScience"],"pagination":["113912"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12648486"],"repository":["biostudies-literature"],"pubmed_title":["A LisH-domain protein interaction map reveals a Lis1-ARIH2-dynein regulatory axis."],"pmcid":["PMC12648486"],"pubmed_authors":["Gupta D","Maddika S"],"additional_accession":[]},"is_claimable":false,"name":"A LisH-domain protein interaction map reveals a Lis1-ARIH2-dynein regulatory axis.","description":"LisH-domain-containing proteins are involved in diverse cellular processes and disease mechanisms, yet their functional interaction landscape remains poorly characterized. Here, we employed a proteomics-based strategy to systematically map the interaction network of 27 LisH-domain-containing proteins, uncovering 1,410 high-confidence interactions-90% of which are previously unreported. This network reveals unanticipated roles for LisH proteins in cellular regulation and uncovers links to human disease, including cancer-associated interactions. Focusing on Lis1, a cytoplasmic dynein regulator, we identify the RBR-E3 ubiquitin ligase ARIH2 as a key functional interactor. We show that Lis1 promotes ARIH2 deneddylation via the COP9 signalosome (CSN), modulating its ubiquitin ligase activity. A","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-05T18:49:43.792Z","creation":"2026-05-20T03:13:38.442Z"},"accession":"S-EPMC12648486","cross_references":{"pubmed":["41312386"],"doi":["10.1016/j.isci.2025.113912"]}}