ArticleiScience2025
A LisH-domain protein interaction map reveals a Lis1-ARIH2-dynein regulatory axis.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
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. Active, neddylated ARIH2 ubiquitinates dynein intermediate chain 1 (DIC1), thus facilitating dynein function in proper organelle positioning. Our findings provide a comprehensive LisH protein interaction network and uncover a regulatory axis involving Lis1-ARIH2 that is important for dynein dependent intracellular transport.
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