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A molecular code for endosomal recycling of phosphorylated cargos by the SNX27–retromer complex

Clairfeuille, Thomas, Mas, Caroline, Chan, Audrey S M, Yang, Zhe, Tello-Lafoz, Maria, Chandra, Mintu, Widagdo, Jocelyn, Kerr, Markus C, Paul, Blessy, Mérida, Isabel, Teasdale, Rohan D, Pavlos, Nathan J, Anggono, Victor, Collins, Brett M·2016·Nature Structural & Molecular Biology
DOI 10.1038/nsmb.3290
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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 [12]

  • 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 [12]

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Research works printed but not linked: 63

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Metadata

Authors
Clairfeuille, T., Mas, C., Chan, A. S. M., Yang, Z., Tello-Lafoz, M., Chandra, M., Widagdo, J., Kerr, M. C., Paul, B., Mérida, I., Teasdale, R. D., Pavlos, N. J., Anggono, V., & Collins, B. M.
ORCID
Venue
Nature Structural & Molecular Biology
Publisher
Springer Science and Business Media LLC
Published
2016-09-05
Volume
23
Issue
10
Pages
921-932
ISSN
  • 1545-9993
  • 1545-9985
DOI
10.1038/nsmb.3290
Cited by
164
References
5
Language
en
Licence
www.springer.com/tdm (tdm)

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