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The Arp2/3 activator WASH regulates α5β1-integrin-mediated invasive migration
Abstract
The actin cytoskeleton provides scaffolding and physical force to effect fundamental processes such as motility, cytokinesis and vesicle trafficking. The Arp2/3 complex nucleates actin structures and contributes to endocytic vesicle invagination and trafficking away from the plasma membrane. Internalisation and directed recycling of integrins are major driving forces for invasive cell motility and potentially for cancer metastasis. Here, we describe a direct requirement for WASH and Arp2/3-mediated actin polymerisation on the endosomal membrane system for α5β1 integrin recycling. WASH regulates the trafficking of endosomal α5β1 integrin to the plasma membrane and is fundamental for integrin-driven cell morphology changes and integrin-mediated cancer cell invasion. Thus, we implicate WASH and Arp2/3-driven actin nucleation in receptor recycling leading to invasive motility.
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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 [13]
The Introduction and the section ‘Integrin recycling is inhibited in WASH-depleted cells’ show that WASH regulates α5β1-integrin recycling and promotes invasive migration. This supports the recycling and migration portions of the claim, but the paper does not establish maintenance of endolysosomal network integrity, exocytosis, or cell adhesion as separate WASH functions. (LLM, conf=0.87)
Experimental — accuracy not yet measuredL2 capsid proteins of various HPV types contain a highly conserved NPxY motif, through which it can engage SNX17, an interaction necessary for viral DNA to avoid lysosomal degradation and reach nucleus.
“Finally, the L2 capsid proteins of various HPV types contain a highly conserved NPxY motif, through which it can engage SNX17, an interaction that is necessary for viral DNA to avoid lysosomal degradation and reach the nucleus53.”
From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [53]
The Introduction and Results and Discussion passages (page numbers unavailable) concern WASH-mediated integrin recycling and invasive migration. Searches for HPV L2, the NPxY motif, SNX17, and viral DNA trafficking found no passage addressing the claimed interaction or its role in avoiding lysosomal degradation and reaching the nucleus. (LLM, conf=0.78)
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Research works printed but not linked: 23
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Cited by
Sorted by citations
Zavodszky, E., Seaman, M. N. J., Moreau, K., Jimenez-Sanchez, M., Breusegem, S. Y., Harbour, M. E., & Rubinsztein, D. C. (2014) · Nature Communications · doi:10.1038/ncomms4828 · Cited by 466
Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3610 · Cited by 346
Endosomal retrieval of cargo: Retromer is not alone
McNally, K. E., & Cullen, P. J. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.005 · Cited by 169
Freeman, C., Seaman, M. N. J., & Reid, E. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.10.011 · Cited by 50
Hereditary spastic paraplegia SPG8 mutations impair CAV1-dependent, integrin-mediated cell adhesion
Lee, S., Park, H., Zhu, P.-P., Jung, S.-Y., Blackstone, C., & Chang, J. (2020) · Science Signaling · doi:10.1126/scisignal.aau7500 · Cited by 22
Metadata
- Authors
- Zech, T., Calaminus, S. D. J., Caswell, P., Spence, H. J., Carnell, M., Insall, R. H., Norman, J., & Machesky, L. M.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2011-11-15
- Volume
- 124
- Issue
- 22
- Pages
- 3753-3759
- ISSN
- 1477-9137
- 0021-9533
- Cited by
- 138
- References
- 0
- Language
- en
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