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Structure of the membrane-assembled retromer coat determined by cryo-electron tomography

Kovtun, Oleksiy, Leneva, Natalya, Bykov, Yury S., Ariotti, Nicholas, Teasdale, Rohan D., Schaffer, Miroslava, Engel, Benjamin D., Owen, David. J., Briggs, John A. G., Collins, Brett M.·2018·Nature
DOI 10.1038/s41586-018-0526-zPMC PMC6173284
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  • 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 [14]

    The paper’s opening section describes retromer generating cargo-selective carriers from endosomal membranes and reports its coat structure on membrane tubules. It does not identify a specialised endosomal nanodomain called the “retrieval sub-domain” or say that such a domain orchestrates retrieval and recycling. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • 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 [14]

  • The precise mechanisms of cargo selection by Retriever have remained elusive.

    “Unlike the well-studied Retromer25,26,34, the precise mechanisms of cargo selection by Retriever have remained elusive37.”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [25]

    The paper’s discussion of cargo binding and sorting concerns Retromer and its associated sorting nexins (section labelled Abstract; page not provided). A search for “Retriever” and “Retriever cargo selection mechanisms” found no passage addressing Retriever or whether its cargo-selection mechanisms remain elusive. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

  • 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 [14]

  • 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 [14]

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Citations

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Research works printed but not linked: 58

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Metadata

Authors
Kovtun, O., Leneva, N., Bykov, Y. S., Ariotti, N., Teasdale, R. D., Schaffer, M., Engel, B. D., Owen, D. J., Briggs, J. A. G., & Collins, B. M.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2018-09
Volume
561
Issue
7724
Pages
561-564
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/s41586-018-0526-z
PMC
PMC6173284
Cited by
247
References
3
Language
en
Licence
www.springer.com/tdm (tdm)

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