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WASH and the Arp2/3 complex regulate endosome shape and trafficking

Duleh, Steve N., Welch, Matthew D.·2010·Cytoskeleton
DOI 10.1002/cm.20437PMC PMC2887680
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Abstract

Activators of the Arp2/3 complex, termed nucleation‐promoting factors (NPFs), are required for the proper spatial and temporal control of actin assembly in cells. Mammalian cells express several NPFs, each of which functions in a distinct cellular process, including WASP and N‐WASP in phagocytosis and endocytosis, WAVE and JMY in cell migration, and WHAMM in ER‐to‐Golgi transport. Although another NPF called WASH was recently identified, the cellular localization and function of this protein were unclear. Here we demonstrated that human WASH alone potently activated the Arp2/3 complex in vitro and in cells, suggesting that the protein is not autoinhibited like N‐WASP, but is likely regulated by interacting proteins. In cells, WASH was associated with Rab5‐positive early endosomes and Rab11‐positive recycling endosomes that were enriched for actin filaments. Silencing of WASH or Arp2/3 complex expression by RNAi, or disruption of actin function by drug treatments, caused enlargement and elongation of endosomes. Intriguingly, WASH silencing, as well as actin disruption, delayed EGF transport to LAMP1‐positive late endosomes. These observations indicate that actin polymerization by WASH influences the shape and maturation of endosomes, and highlight a previously unrecognized role for WASH and the Arp2/3 complex in the degradative steps of endocytic trafficking. © 2010 Wiley‐Liss, Inc.

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  • Regulation of branched F-actin formation by WASH is needed for proper morphology of the endolysosomal system and endosomal trafficking of a broad range of cargoes.

    “Regulation of branched F-actin formation by WASH is needed for proper morphology of the endolysosomal system and endosomal trafficking of a broad range of cargoes37,39,41–44”

    From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [41]

    The Results show that disrupting WASH, Arp2/3, or actin alters endosome shape, and that WASH depletion delays EGF transport to late endosomes (page not available in our copy). The Discussion also says WASH depletion did not affect transferrin uptake or recycling. Thus the paper supports a role in endosome morphology and trafficking of EGF, but not the claim that WASH is needed for trafficking a broad range of cargoes throughout the endolysosomal system. (LLM, conf=0.88)

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  • WASH is recruited to endosomes where it is necessary for branched F-actin deposition, a process essential to maintain endolysosomal network structure, promote fission of membrane tubules, and traffic cargo proteins.

    “WASH is recruited to endosomes where it is necessary for branched F-actin deposition, a process that is essential to maintain the structure of the endolysosomal network, to promote effective fission of membrane tubules and trafficking of cargo proteins37,39,41,43,44.”

    From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [41]

    The Introduction and Results report WASH on endosomes, a role for WASH and actin in maintaining endosome shape, and reduced EGF transport to late endosomes after WASH depletion. The Discussion says that actin assembly might sever endosomal tubules, but explicitly presents fission as speculation, not an established essential process. The paper also studies particular endosomal compartments and EGF trafficking rather than establishing a requirement across the entire endolysosomal network and cargo proteins generally. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

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Metadata

Authors
Duleh, S. N., & Welch, M. D.
Venue
Cytoskeleton
Publisher
Wiley
Published
2010-02-19
Volume
67
Issue
3
Pages
193-206
ISSN
  • 1949-3584
  • 1949-3592
DOI
10.1002/cm.20437
PMC
PMC2887680
Cited by
207
References
3
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor)

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