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A FAM21-Containing WASH Complex Regulates Retromer-Dependent Sorting

Gomez, Timothy S., Billadeau, Daniel D.·2009·Developmental Cell

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Crossref · 10.1016/j.devcel.2009.09.009

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  • Mammalian cells lacking strumpellin have an increased number of SNX1- and VPS26-positive endosomal tubules.

    “Mammalian cells lacking strumpellin have an increased number of SNX1- and VPS26-positive endosomal tubules [9,10,13].”

    From The hereditary spastic paraplegia protein strumpellin: Characterisation in neurons and of the effect of disease mutations on WASH complex assembly and function (2013) · cites this paper as [10]

    The Results section, “Retromer-mediated tubulation is exaggerated in the absence of WASH” (page unavailable), reports elongated VPS29-rich endosomal tubules after WASH depletion and describes SNX1 localization to endosomes. It does not establish the claimed increase in SNX1- and VPS26-positive tubules in cells lacking strumpellin; the tested depletion and VPS marker differ. (LLM, conf=0.82)

    Experimental — accuracy not yet measured
  • The WASH complex functions in endocytic recycling, maintenance of endolysosomal network integrity, exocytosis, cell adhesion, and cell migration.

    “The WASH complex functions in the endocytic recycling of various types of membrane proteins, maintenance of endolysosomal network integrity, exocytosis, cell adhesion, and cell migration (11-23).”

    From Hereditary spastic paraplegia SPG8 mutations impair CAV1-dependent, integrin-mediated cell adhesion (2020) · cites this paper as [12]

    The Results section on CI-MPR sorting shows that WASH regulates retromer-dependent transport of a membrane receptor from endosomes toward the Golgi, supporting a role in endosomal recycling. The paper does not establish the broader claims about maintenance of endolysosomal network integrity, exocytosis, cell adhesion, or cell migration; it also reports that WASH is dispensable for TCR and EGFR endocytosis. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • The common labelling of the WASH complex by both Retromer and Retriever is consistent with their known biochemical association and physical co-localisation to the retrieval sub-domain and the central role of actin polymerisation and actin turnover in Retromer- and Retriever-dependent cargo sorting.

    “Building on this, the common labelling of the WASH complex by both Retromer and Retriever (Fig. 2E) is entirely consistent with their known biochemical association and physical co-localisation to the retrieval sub-domain and the central role of actin polymerisation and actin turnover in Retromer- and Retriever-dependent cargo sorting17,19,24,56–58.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [24]

    Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.

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  • WASH serves as an actin nucleation-promoting factor for the ARP2/3 complex, which drives the generation of branched F-actin filaments on endosomal membranes.

    “WASH serves as an actin nucleation-promoting factor for the ARP2/3 complex, which drives the generation of branched F-actin filaments on endosomal membranes37–40”
  • The WASH complex is recruited to endosomes by interactions with the retromer complex.

    “Strumpellin is a component of the WASH complex, an actin-regulating complex that is recruited to endosomes by interactions with the retromer complex.”

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Research works printed but not linked: 39

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  2. Bonifacino, 2008, Retromer, Curr. Opin. Cell Biol., 20, 427, 10.1016/j.ceb.2008.03.009 · DOI · Paper page
  3. Campellone, 2008, WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport, Cell, 134, 148, 10.1016/j.cell.2008.05.032 · DOI
  4. Carlton, 2004, Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides, Curr. Biol., 14, 1791, 10.1016/j.cub.2004.09.077 · DOI · Paper page
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  8. Derivery, 2009, The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex, Dev. Cell, 17, 712, 10.1016/j.devcel.2009.09.010 · DOI · Paper page
  9. Gautreau, 2004, Purification and architecture of the ubiquitous Wave complex, Proc. Natl. Acad. Sci. USA, 101, 4379, 10.1073/pnas.0400628101 · DOI
  10. Goley, 2006, The ARP2/3 complex: an actin nucleator comes of age, Nat. Rev. Mol. Cell Biol., 7, 713, 10.1038/nrm2026 · DOI
  11. Gomez, 2008, T cell activation and the cytoskeleton: you can't have one without the other, Adv. Immunol., 97, 1, 10.1016/S0065-2776(08)00001-1 · DOI
  12. Gomez, 2005, Dynamin 2 regulates T cell activation by controlling actin polymerization at the immunological synapse, Nat. Immunol., 6, 261, 10.1038/ni1168 · DOI
  13. Gomez, 2007, Formins regulate the actin-related protein 2/3 complex-independent polarization of the centrosome to the immunological synapse, Immunity, 26, 177, 10.1016/j.immuni.2007.01.008 · DOI
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  15. Gullapalli, 2004, A role for sorting nexin 2 in epidermal growth factor receptor down-regulation: evidence for distinct functions of sorting nexin 1 and 2 in protein trafficking, Mol. Biol. Cell, 15, 2143, 10.1091/mbc.e03-09-0711 · DOI
  16. Haft, 2000, Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes, Mol. Biol. Cell, 11, 4105, 10.1091/mbc.11.12.4105 · DOI · Paper page
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  21. Linardopoulou, 2007, Human subtelomeric WASH genes encode a new subclass of the WASP family, PLoS Genet., 3, e237, 10.1371/journal.pgen.0030237 · DOI
  22. Liu, 2009, Wash functions downstream of Rho and links linear and branched actin nucleation factors, Development, 136, 2849, 10.1242/dev.035246 · DOI
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Metadata

Authors
Gomez, T. S., & Billadeau, D. D.
Venue
Developmental Cell
Publisher
Elsevier BV
Published
2009-11
Volume
17
Issue
5
Pages
699-711
ISSN
1534-5807
Cited by
521
References
0
Language
en
Funders
  • National Institutes of Health (NIH-T32-AI07047, R01-AI065474)
  • Mayo Foundation for Medical Education and Research

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