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Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly
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Abstract
Cryo–electron tomography shows how retromer recruits cargo and tubulates endosomes without canonical membrane-bending proteins.
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Endosomal cargo retrieval and recycling are orchestrated by several multi-protein assemblies including SNX27-Retromer and SNX3-Retromer, SNX17-Retriever and associated Commander super-assembly, the WASH complex and its regulatory MUST complex, and the SNX-BAR proteins and ESCPE-1.
“Orchestrating endosomal cargo retrieval and recycling are several multi-protein assemblies that include sorting nexin-27 (SNX27)-Retromer and SNX3-Retromer8–16, SNX17-Retriever and associated Commander super-assembly17–22, the branched F-actin polymerising WASH complex and its regulatory MAGE-L2/USP7/TRIM27 (MUST) complex23–25, and the SNX-BAR proteins and endosomal sorting complex required for ex”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [16]
Retromer is approximately 15-20 nm in length.
“for context Retromer is approximately 15–20 nm in length14,16”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [16]
Cryo-ET analysis of membrane-associated Retromer has established a polarised organisation where the amino-terminal region of VPS35 associates with VPS26A/B proximal to the membrane surface and the membrane distal carboxy-terminal region of VPS35 dimerises with a neighbouring Retromer to form an arch-like structure.
“Cryo-ET analysis of membrane-associated Retromer has established a polarised organisation where the amino-terminal region of VPS35 associates with VPS26A/B proximal to the membrane surface and the membrane distal carboxy-terminal region of VPS35 dimerises with a neighbouring Retromer to form an arch-like structure (Fig. 2F and Supplementary Fig. 4B)13,14,16.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [16]
Endosomal retrieval and recycling is orchestrated through a specialised endosomal nanodomain, the retrieval sub-domain.
“and is orchestrated through a specialised endosomal nanodomain, the retrieval sub-domain”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [16]
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Citations
Cites
Retromer: A Master Conductor of Endosome Sorting
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Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
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Endosomal retrieval of cargo: Retromer is not alone
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TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats
Ma, W., & Goldberg, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605916113 · Cited by 108
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Butkovič, R., Walker, A. P., Healy, M. D., McNally, K. E., Liu, M., Veenendaal, T., Kato, K., Liv, N., Klumperman, J., Collins, B. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50971-0 · Cited by 26
Structural basis for Retriever-SNX17 assembly and endosomal sorting
Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23
Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation
Antón-Plágaro, C., Chen, K.-E., Guo, Q., Liu, M., Evans, A. J., Lewis, P. A., Heesom, K. J., Wilkinson, K. A., Collins, B. M., & Cullen, P. J. (2025) · Nature Communications · doi:10.1038/s41467-025-61802-1 · Cited by 14
Metadata
- Authors
- Leneva, N., Kovtun, O., Morado, D. R., Briggs, J. A. G., & Owen, D. J.
- Affiliations
- Cambridge Institute for Medical Research, Cambridge Biomedical Campus, Hills Road, Cambridge CB2 0XY, UK.
- MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
- Venue
- Science Advances
- Published
- 2021-03-26
- Volume
- 7
- Issue
- 13
- ISSN
- 2375-2548
- PMC
- PMC7990337
- Cited by
- 90
- References
- 4
- Language
- en
- Funders
- Wellcome (207455/Z/17/Z, 206171/Z/17/Z, 202905/Z/16/Z)
- H2020 European Research Council (ERC-CoG-648432 MEMBRANEFUSION)
- Medical Research Council (MC_UP_1201/16)
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