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May the force be with you: Myosin-X in phagocytosis

Engulfment of pathogens by phagocytosis requires the coordination of actin assembly and progressive 'zippering' of pseudopodial membranes around the particle. Recent work shows that Myosin-X, which binds phosphatidylinositol-3-OH kinase (PI(3)K) products through its pleckstrin homology (PH) domains, is required for phagocytosis, thereby providing a molecular basis for the function of PI(3)K in pseudopod extension.

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Figure 1: A model for PI(3)K-dependent function of Myosin-X during phagocytosis.

References

  1. Aderem, A. & Underhill, D. M. Annu. Rev. Immunol. 17, 593–623 (1999).

    Article  CAS  Google Scholar 

  2. Castellano, F., Chavrier, P. & Caron, E. Semin. Immunol. 13, 347–355 (2001).

    Article  CAS  Google Scholar 

  3. Cox, D. & Greenberg, S. Semin. Immunol. 13, 339–345 (2001).

    Article  CAS  Google Scholar 

  4. Cox, D. et al. Nature Cell Biol. 4, 469–477 (2002).

    Article  CAS  Google Scholar 

  5. Marshall, J. G. et al. J. Cell Biol. 153, 1369–1380 (2001).

    Article  CAS  Google Scholar 

  6. Araki, N., Johnson, M. T. & Swanson, J. A. J. Cell. Biol. 135, 1249–1260 (1996).

    Article  CAS  Google Scholar 

  7. Cox, D., Tseng, C. C., Bjekic, G. & Greenberg, S. J. Biol. Chem. 274, 1240–1247 (1999).

    Article  CAS  Google Scholar 

  8. Hackam, D. J. et al. Proc. Natl Acad. Sci. USA 95, 11691–11696 (1998).

    Article  CAS  Google Scholar 

  9. Bajno, L. et al. J. Cell Biol. 149, 697–706 (2000).

    Article  CAS  Google Scholar 

  10. Booth, J. W., Trimble, W. S. & Grinstein, S. Semin. Immunol. 13, 357–364 (2001).

    Article  CAS  Google Scholar 

  11. Swanson, J. A. et al. J. Cell Sci. 112, 307–316 (1999).

    CAS  PubMed  Google Scholar 

  12. Evans, E., Leung, A. & Zhelev, D. J. Cell Biol. 122, 1295–1300 (1993).

    Article  CAS  Google Scholar 

  13. Allen, L. H. & Aderem, A. J. Exp. Med. 182, 829–840 (1995).

    Article  CAS  Google Scholar 

  14. Diakonova, M., Bokoch, G. & Swanson, J. A. Mol. Biol. Cell 13, 402–411 (2002).

    Article  CAS  Google Scholar 

  15. Berg, J. S., Derfler, B. H., Pennisi, C. M., Corey, D. P. & Cheney, R. E. J. Cell Sci. 113, 3439–3451 (2000).

    CAS  Google Scholar 

  16. Berg, J. S., Powell, B. C. & Cheney, R. E. Mol. Biol. Cell 12, 780–794 (2001).

    Article  CAS  Google Scholar 

  17. Isakoff, S. J. et al. EMBO J. 17, 5374–5387 (1998).

    Article  CAS  Google Scholar 

  18. Berg, J. S. & Cheney, R. E. Nature Cell Biol. 4, 246–250 (2002).

    Article  CAS  Google Scholar 

  19. Homma, K., Saito, J., Ikebe, R. & Ikebe, M. J. Biol. Chem. 276, 34348–34354 (2001).

    Article  CAS  Google Scholar 

  20. Titus, M. A. Curr. Biol. 9, 1297–1303 (1999).

    Article  CAS  Google Scholar 

  21. Tuxworth, R. I. et al. Curr. Biol. 11, 318–329 (2001).

    Article  CAS  Google Scholar 

  22. Bretscher, M. S. Cell 87, 601–606 (1996).

    Article  CAS  Google Scholar 

Download references

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Chavrier, P. May the force be with you: Myosin-X in phagocytosis. Nat Cell Biol 4, E169–E171 (2002). https://doi.org/10.1038/ncb0702-e169

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