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Sequence-Dependent Sorting of Recycling Proteins by Actin-Stabilized Endosomal Microdomains

Puthenveedu, Manojkumar A., Lauffer, Benjamin, Temkin, Paul, Vistein, Rachel, Carlton, Peter, Thorn, Kurt, Taunton, Jack, Weiner, Orion D., Parton, Robert G., von Zastrow, Mark·2010·Cell
DOI 10.1016/j.cell.2010.10.003PMC PMC3058345
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Crossref · 10.1016/j.cell.2010.10.003

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  • Specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches.

    “A number of studies have shown that specific endosomal membrane sub-domains are enriched for either degradative components such as ESCRT or recycling machinery including Retromer, Retriever, the CCC complex, and WASH-dependent actin patches9,34–44”

    From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [34]

    The Discussion describes ESCRT-associated degradative domains and distinct actin-stabilized recycling tubules; the Results report WASH localized to those tubules (page numbers unavailable). The paper does not establish that recycling there is WASH-dependent, describes further specialization of the retromer pathway only as a possibility, and does not address Retriever or the CCC complex. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Core retrieval and recycling complexes localise to specific retrieval sub-domains that are physically distinct from ESCRT-demarcated degradative sub-domains on the same endosome.

    “On the limiting membrane of endosomes, electron and light microscopy has established that core retrieval and recycling complexes localise to specific retrieval sub-domains that, while present on the same endosome, are physically distinct from ESCRT-demarcated degradative sub-domains19,32–37.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [34]

    The Discussion (page unavailable) identifies specialized recycling tubules and describes them as complementary to ESCRT-associated domains on the vacuolar portion of endosomes. It does not establish that core retrieval and recycling complexes localise to those tubules; the ESCRT comparison is presented as a proposed sorting mechanism, not as a directly demonstrated localisation result. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • The study's proximity proteomic analysis established a clear biochemical separation in the proximity profile of the HRS-demarcated degradative sub-domain and the Retromer/Retriever-defined retrieval sub-domain.

    “This has established a clear biochemical separation in the proximity profile of these degradative and retrieval sub-domains, entirely consistent with imaging data of their spatial separation on the limiting membrane of individual endosomes34.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [34]

    The Results ('Visualization of receptor sorting in the endosomes of living cells'; page unavailable) report imaging-based separation of a recycling receptor from a degrading receptor, supporting the cited sentence's reference to spatial separation. The paper does not establish the claimed proximity-proteomic separation of HRS-demarcated and Retromer/Retriever-defined sub-domains; its Discussion describes further specialization of degradative and retromer-based pathways as a possibility. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • These foci represent previously described retrieval sub-domains from where cargo-enriched transport carriers exit the endosome.

    “These foci therefore represent the previously described retrieval sub-domains from where cargo-enriched transport carriers exit the endosome for transport to their destination9,34,35,39,41,49.”

    From Mechanism and regulation of cargo entry into the Commander endosomal recycling pathway (2024) · cites this paper as [34]

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Citations

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Metadata

Authors
Puthenveedu, M. A., Lauffer, B., Temkin, P., Vistein, R., Carlton, P., Thorn, K., Taunton, J., Weiner, O. D., Parton, R. G., & von Zastrow, M.
Venue
Cell
Publisher
Elsevier BV
Published
2010-11
Volume
143
Issue
5
Pages
761-773
ISSN
0092-8674
DOI
10.1016/j.cell.2010.10.003
PMC
PMC3058345
Cited by
317
References
4
Language
en
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