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Structural Mechanism for Cargo Recognition by the Retromer Complex

Lucas, María, Gershlick, David C., Vidaurrazaga, Ander, Rojas, Adriana L., Bonifacino, Juan S., Hierro, Aitor·2016·Cell
DOI 10.1016/j.cell.2016.10.056PMC PMC5147500
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Crossref · 10.1016/j.cell.2016.10.056

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  • This interaction is unique to Retriever, as Retromer uses distinct surfaces to interact with adaptors, such as SNX3 and SNX27, or directly with cargoes, such as DMT1.

    “This interaction is unique to Retriever, as Retromer uses distinct surfaces to interact with adaptors, such as SNX3 and SNX27, or directly with cargoes, such as DMT126,29,34”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [26]

    The Introduction and Results describe SNX3 binding retromer through VPS26–VPS35 interfaces and DMT1-II cargo recognition at a VPS26–SNX3 interface. The paper mentions SNX27 but does not establish its retromer-binding surface or compare these interactions with Retriever. It also finds that DMT1-II binding requires SNX3, qualifying the claim of direct cargo binding. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Various sorting nexin proteins, such as SNX27, SNX32, SNX1-SNX6, and SNX1-SNX5, are autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.

    “Interestingly, various sorting nexin proteins, such as SNX2729, SNX326,39, SNX1-SNX628, and SNX1-SNX540, operate similarly, being autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [26]

    The Results section (“DMT1-II Binding is Concomitant With Interaction of SNX3 with Retromer”; page unavailable) reports that SNX3 binds retromer in the presence of cargo but has no detectable affinity without it. The paper does not establish basal-state autoinhibition or the same cargo-dependent behavior for the other listed sorting nexins. The printed “SNX326,39” appears to denote SNX3 followed by citation numbers, rather than SNX32. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • The SNX3-Retromer assembly is essential for the sequence-dependent retrieval and recycling of cargoes.

    “An additional cargo adaptor complex essential for the sequence-dependent retrieval and recycling of cargoes is the sorting nexin-3 (SNX3)-Retromer assembly [25,30,66,67].”

    From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [66]

    The Introduction identifies a binding site for canonical recycling signals at the VPS26–SNX3 interface. The Results section on DMT1-II binding shows that SNX3–retromer interactions are required to sort DMT1-II out of endosomes into recycling intermediates. The paper does not establish that this assembly is essential for retrieval and recycling of cargoes generally. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • SNX3 directly binds to a subset of cargo containing the sequence motif [+/-]-x-∅-x-[L/M], with many of these cargoes trafficked through the retrograde endosome-to-TGN pathway.

    “SNX3 directly binds to a subset of cargo containing the poorly defined sequence motif [+/-]-x-∅-x-[L/M] (∅ -bulky aromatic residue) with many of these cargoes trafficked through the retrograde endosome-to-TGN pathway [25,30,66,67].”

    From Global identification of neuronal and astrocytic integral membrane proteins that require Retromer for their endosomal recycling (2026) · cites this paper as [66]

    The Results section, “A Mechanism for Cargo Recognition” (page unavailable), shows that the DMT1-II recycling signal contacts SNX3 and VPS26 at a binding site for a related ØX(L/M) motif. But “DMT1-II Binding is Concomitant With Interaction of SNX3 with Retromer” reports no detectable binding to isolated SNX3. The paper describes DMT1-II cycling between endosomes and the plasma membrane; although the Introduction says retromer also transports cargo to the TGN, it does not establish that many SNX3-recognized cargoes take that route. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • 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 [13]

    The Introduction (page unavailable) says retromer recycles cargo from endosomes through tubular-vesicular carriers, and the Discussion describes how membrane recruitment and cargo recognition cooperate. The copy does not identify a specialised endosomal nanodomain called the “retrieval sub-domain” or say that it orchestrates recycling. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Citations

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Metadata

Authors
Lucas, M., Gershlick, D. C., Vidaurrazaga, A., Rojas, A. L., Bonifacino, J. S., & Hierro, A.
Venue
Cell
Publisher
Elsevier BV
Published
2016-12
Volume
167
Issue
6
Pages
1623-1635.e14
ISSN
0092-8674
DOI
10.1016/j.cell.2016.10.056
PMC
PMC5147500
Cited by
223
References
2
Language
en
Licence
Funders
  • Carlos III Health Institute (PI11/00121)
  • Basque Government (PI2011-26)
  • Spanish Ministry of Economy and Competitiveness (BFU2014-59759-R)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH (ZIA HD001607)
  • European Community’s Seventh Framework Programme (FP7/2007-2013, 283570)

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