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Cited by 60

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Retromer Endosome Exit Domains Serve Multiple Trafficking Destinations and Regulate Local G Protein Activation by GPCRs

Varandas, Katherine C., Irannejad, Roshanak, von Zastrow, Mark·2016·Current Biology
DOI 10.1016/j.cub.2016.09.052PMC PMC5140749
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Crossref · 10.1016/j.cub.2016.09.052

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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 [41]

    The Results describe retromer endosome domains containing recycling and retrograde cargos, supporting the Retromer portion of the citing sentence. The passages do not establish enrichment of ESCRT, Retriever, the CCC complex, or WASH-dependent actin patches in distinct endosomal sub-domains. (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 [36]

    The Results section ('Flag-β2AR and HA-Wls transit the same endosomes and retromer endosome domains'; page unavailable) shows recycling and retrograde cargos associating with retromer domains on the same endosomes. Our copy does not establish that these domains are physically distinct from ESCRT-demarcated degradative domains, or attribute that distinction to electron microscopy. (LLM, conf=0.84)

    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 [41]

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Citations

Cites

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Research works printed but not linked: 44

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  12. Swarbrick, 2011, VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins, PLoS ONE, 6, e20420, 10.1371/journal.pone.0020420 · DOI · Paper page
  13. Harterink, 2011, A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion, Nat. Cell Biol., 13, 914, 10.1038/ncb2281 · DOI · Paper page
  14. Zhang, 2011, SNX3 controls Wingless/Wnt secretion through regulating retromer-dependent recycling of Wntless, Cell Res., 21, 1677, 10.1038/cr.2011.167 · DOI
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Metadata

Authors
Varandas, K. C., Irannejad, R., & von Zastrow, M.
Venue
Current Biology
Publisher
Elsevier BV
Published
2016-12
Volume
26
Issue
23
Pages
3129-3142
ISSN
0960-9822
DOI
10.1016/j.cub.2016.09.052
PMC
PMC5140749
Cited by
60
References
3
Language
en
Licence
Funders
NIH (DA036290, HL122508, DA012864, DA010711)

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