ArticlebioRxiv : the preprint server for biology2026
Structural Mechanisms of DNAJC13 Dimeric Assembly and InsP
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
5 authors.
Funding
Abstract
The balance of plasma membrane protein degradation and recycling during endocytosis is regulated, in part, by the large J-domain-containing protein DNAJC13/RME-8 and WASH complexes, which function together with Retromer to support cargo trafficking into recycling endosomes. Despite extensive cellular and biochemical studies, the structural basis and proteomic landscape of DNAJC13 function remain elusive. Here, we find that DNAJC13 forms an unexpected antiparallel homodimeric architecture involving distinctive symmetrical interactions between composite IWN1 and α-solenoid ARM2 domains in each protomer. Additionally, two PH-like domains of unknown function (PHL2 and PHL3), adjacent to the PI(3)P-binding PHL1 domain, form an unanticipated composite, positively charged pocket occupied by InsP
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Registered trials
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