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The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIα

Ryder, P. V., Vistein, R., Gokhale, A., Seaman, M. N., Puthenveedu, M. A., Faundez, V.·2013·Molecular Biology of the Cell
DOI 10.1091/mbc.e13-02-0088PMC PMC3708732
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Abstract

Vesicle biogenesis machinery components such as coat proteins can interact with the actin cytoskeleton for cargo sorting into multiple pathways. It is unknown, however, whether these interactions are a general requirement for the diverse endosome traffic routes. In this study, we identify actin cytoskeleton regulators as previously unrecognized interactors of complexes associated with the Hermansky–Pudlak syndrome. Two complexes mutated in the Hermansky–Pudlak syndrome, adaptor protein complex-3 and biogenesis of lysosome-related organelles complex-1 (BLOC-1), interact with and are regulated by the lipid kinase phosphatidylinositol-4-kinase type IIα (PI4KIIα). We therefore hypothesized that PI4KIIα interacts with novel regulators of these complexes. To test this hypothesis, we immunoaffinity purified PI4KIIα from isotope-labeled cell lysates to quantitatively identify interactors. Strikingly, PI4KIIα isolation preferentially coenriched proteins that regulate the actin cytoskeleton, including guanine exchange factors for Rho family GTPases such as RhoGEF1 and several subunits of the WASH complex. We biochemically confirmed several of these PI4KIIα interactions. Of importance, BLOC-1 complex, WASH complex, RhoGEF1, or PI4KIIα depletions altered the content and/or subcellular distribution of the BLOC-1–sensitive cargoes PI4KIIα, ATP7A, and VAMP7. We conclude that the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo PI4KIIα interact with regulators of the actin cytoskeleton.

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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 [44]

    The Results and Discussion (page unavailable) place WASH and actin on early endosomes and report elongated endosomal tubules and cargo missorting after WASH depletion. The paper supports a role in endosomal morphology and cargo trafficking, but describes WASH-driven membrane scission as a hypothesis awaiting testing; it does not establish that this process is essential to maintain the structure of the endolysosomal network. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • 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 [44]

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Metadata

Authors
Ryder, P. V., Vistein, R., Gokhale, A., Seaman, M. N., Puthenveedu, M. A., & Faundez, V.
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2013-07-15
Volume
24
Issue
14
Pages
2269-2284
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e13-02-0088
PMC
PMC3708732
Cited by
87
References
6
Language
en

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