ArticlebioRxiv : the preprint server for biology2026
Cargo-Adaptor Cooperation Programs Retromer Coat Architecture.
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
8 authors.
Funding
Abstract
Retromer drives endosomal cargo retrieval in combination with sorting nexin (SNX) adaptors, but how adaptor-cargo combinations specify coat architecture remains unclear. We identify sorting nexin 12 (SNX12) as the retromer adaptor required for human papillomavirus 16 (HPV16) infection and show that the viral L2 capsid protein tail directly engages SNX12-retromer complexes to trigger membrane tubulation. The crystal structure reveals a conserved cargo-recognition mode, whereas cryo-electron tomography of reconstituted assemblies shows retromer arches organized into two lattice configurations stabilized by membrane-proximal interfaces. These lattices assemble as multi-start helices and accommodate curvature through hinge-like motions between arches. These findings establish cargo and adaptor identity as co-determinants of retromer coat architecture, revealing retromer as a programmable system capable of generating route-specific transport carriers.
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Registered trials
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