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Myosin IIA Associates with NK Cell Lytic Granules to Enable Their Interaction with F-Actin and Function at the Immunological Synapse
Abstract
NK cell cytotoxicity requires the formation of an actin-rich immunological synapse (IS) with a target cell and the polarization of perforin-containing lytic granules toward the IS. Following the polarization of lytic granules, they traverse through the actin-rich IS to join the NK cell membrane in order for directed secretion of their contents to occur. We examined the role of myosin IIA as a candidate for facilitating this prefinal step in lytic NK cell IS function. Lytic granules in and derived from a human NK cell line, or ex vivo human NK cells, were constitutively associated with myosin IIA. When isolated using density gradients, myosin IIA-associated NK cell lytic granules directly bound to F-actin and the interaction was sensitive to the presence of ATP under conditions of flow. In NK cells from patients with a truncation mutation in myosin IIA, NK cell cytotoxicity, lytic granule penetration into F-actin at the IS, and interaction of isolated granules with F-actin were all decreased. Similarly, inhibition of myosin function also diminished the penetration of lytic granules into F-actin at the IS, as well as the final approach of lytic granules to and their dynamics at the IS. Thus, NK cell lytic granule-associated myosin IIA enables their interaction with actin and final transit through the actin-rich IS to the synaptic membrane, and can be defective in the context of naturally occurring human myosin IIA mutation.
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“Therefore, our data confirm the previously reported function of myosin IIA in terms of translocation of granules and mitochondria in other cell types such as NK cells and thrombocytes [46–49].”
From Nascent RHOH acts as a molecular brake on actomyosin-mediated effector functions of inflammatory neutrophils (2022) · cites this paper as [47]
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Cites
Functions of natural killer cells
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Cook, S. A., Comrie, W. A., Poli, M. C., Similuk, M., Oler, A. J., Faruqi, A. J., Kuhns, D. B., Yang, S., Vargas-Hernández, A., Carisey, A. F., et al. (2020) · Science · doi:10.1126/science.aay5663 · Cited by 102
Self-citationSubstance P inhibits natural killer cell cytotoxicity through the neurokinin-1 receptor
Monaco-Shawver, L., Schwartz, L., Tuluc, F., Guo, C.-J., Lai, J. P., Gunnam, S. M., Kilpatrick, L. E., Banerjee, P. P., Douglas, S. D., & Orange, J. S. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0410200 · Cited by 39
Self-citationPeng, S., Stojkov, D., Gao, J., Oberson, K., Latzin, P., Casaulta, C., Yousefi, S., & Simon, H.-U. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001794 · Cited by 15
Metadata
- Authors
- Sanborn, K. B., Rak, G. D., Maru, S. Y., Demers, K., Difeo, A., Martignetti, J. A., Betts, M. R., Favier, R., Banerjee, P. P., & Orange, J. S.
- Affiliations
- Immunology Graduate Group, University of Pennsylvania School of Medicine , Philadelphia, PA 19104
- Cell Biology and Physiology Graduate Program, University of Pennsylvania School of Medicine , Philadelphia, PA 19104
- Joseph Stokes Jr. Research Institute of the Children’s Hospital of Philadelphia , Philadelphia, PA 19104
- Department of Microbiology, University of Pennsylvania , Philadelphia, PA 19104
- Department of Genetics and Genomic Sciences, Mount Sinai School of Medicine , New York, NY 10029
- Assistance Publique-Hôpitaux de Paris, Centre de Référence des Pathologies Plaquettaires, Armand Trousseau Children’s Hospital , 75012; INSERM U790, Villejuif,
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-06-01
- Volume
- 182
- Issue
- 11
- Pages
- 6969-6984
- ISSN
- 1550-6606
- 0022-1767
- PMC
- PMC2835774
- Cited by
- 87
- References
- 1
- Language
- en
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