SEARCH

SEARCH BY CITATION

References

  • Bennett, R.D., Mauer, A.S., and Strehler, E.E. (2007) Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J Biol Chem 282: 32053212.
  • Bennish, M.L., and Wojtyniak, B.J. (1991) Mortality due to shigellosis: community and hospital data. Rev Infect Dis 13 (Suppl. 4): S245S251.
  • Berg, J.S., and Cheney, R.E. (2002) Myosin-X is an unconventional myosin that undergoes intrafilopodial motility. Nat Cell Biol 4: 246250.
  • Berg, J.S., Derfler, B.H., Pennisi, C.M., Corey, D.P., and Cheney, R.E. (2000) Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin. J Cell Sci 113 (Part 19): 34393451.
  • Berg, J.S., Powell, B.C., and Cheney, R.E. (2001) A millennial myosin census. Mol Biol Cell 12: 780794.
  • Bohil, A.B., Robertson, B.W., and Cheney, R.E. (2006) Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci USA 103: 1241112416.
  • Cox, D., Berg, J.S., Cammer, M., Chinegwundoh, J.O., Dale, B.M., Cheney, R.E., and Greenberg, S. (2002) Myosin X is a downstream effector of PI(3)K during phagocytosis. Nat Cell Biol 4: 469477.
  • Finlay, B.B., and Falkow, S. (1997) Common themes in microbial pathogenicity revisited. Microbiol Mol Biol Rev 61: 136169.
  • Goldberg, M.B., Theriot, J.A., and Sansonetti, P.J. (1994) Regulation of surface presentation of IcsA, a Shigella protein essential to intracellular movement and spread, is growth phase dependent. Infect Immun 62: 56645668.
  • Gupton, S.L., and Gertler, F.B. (2007) Filopodia: the fingers that do the walking. Sci STKE 2007: re5.
  • Hartwig, J.H. (1992) Mechanisms of actin rearrangements mediating platelet activation. J Cell Biol 118: 14211442.
  • Kerber, M.L., and Cheney, R.E. (2011) Myosin-X: a MyTH-FERM myosin at the tips of filopodia. J Cell Sci 124: 37333741.
  • Kerber, M.L., Jacobs, D.T., Campagnola, L., Dunn, B.D., Yin, T., Sousa, A.D., et al. (2009) A novel form of motility in filopodia revealed by imaging myosin-X at the single-molecule level. Curr Biol 19: 967973.
  • Kotloff, K.L., Winickoff, J.P., Ivanoff, B., Clemens, J.D., Swerdlow, D.L., Sansonetti, P.J., et al. (1999) Global burden of Shigella infections: implications for vaccine development and implementation of control strategies. Bull World Health Organ 77: 651666.
  • Liu, K.C., Jacobs, D.T., Dunn, B.D., Fanning, A.S., and Cheney, R.E. (2012) Myosin-X functions in polarized epithelial cells. Mol Biol Cell 23: 16751687.
  • Lu, Q., Yu, J., Yan, J., Wei, Z., and Zhang, M. (2011) Structural basis of the myosin X PH1N-PH2-PH1C tandem as a specific and acute cellular PI(3,4,5)P3 sensor. Mol Biol Cell 22: 42684278.
  • Mashanov, G.I., Tacon, D., Peckham, M., and Molloy, J.E. (2004) The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts. J Biol Chem 279: 1527415280.
  • Meitert, T., Pencu, E., Ciudin, L., Tonciu, M., Mihai, I., and Nicolescu, S. (1991) Correlation between Congo red binding as virulence marker in Shigella species and Sereny test. Roum Arch Microbiol Immunol 50: 4552.
  • Oaks, E.V., Wingfield, M.E., and Formal, S.B. (1985) Plaque formation by virulent Shigella flexneri. Infect Immun 48: 124129.
  • Plantard, L., Arjonen, A., Lock, J.G., Nurani, G., Ivaska, J., and Stromblad, S. (2010) PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation. J Cell Sci 123: 35253534.
  • Pust, S., Morrison, H., Wehland, J., Sechi, A.S., and Herrlich, P. (2005) Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell. EMBO J 24: 12871300.
  • Rogers, M.S., and Strehler, E.E. (2001) The tumor-sensitive calmodulin-like protein is a specific light chain of human unconventional myosin X. J Biol Chem 276: 1218212189.
  • Sansonetti, P.J. (2001) Microbes and microbial toxins: paradigms for microbial-mucosal interactions III. Shigellosis: from symptoms to molecular pathogenesis. Am J Physiol Gastrointest Liver Physiol 280: G319G323.
  • Sansonetti, P.J., Arondel, J., Fontaine, A., d'Hauteville, H., and Bernardini, M.L. (1991) OmpB (osmo-regulation) and icsA (cell-to-cell spread) mutants of Shigella flexneri: vaccine candidates and probes to study the pathogenesis of shigellosis. Vaccine 9: 416422.
  • Sidhu, G., Li, W., Laryngakis, N., Bishai, E., Balla, T., and Southwick, F. (2005) Phosphoinositide 3-kinase is required for intracellular Listeria monocytogenes actin-based motility and filopod formation. J Biol Chem 280: 1137911386.
  • Stevens, J.M., Galyov, E.E., and Stevens, M.P. (2006) Actin-dependent movement of bacterial pathogens. Nat Rev Microbiol 4: 91101.
  • Umeki, N., Jung, H.S., Sakai, T., Sato, O., Ikebe, R., and Ikebe, M. (2011) Phospholipid-dependent regulation of the motor activity of myosin X. Nat Struct Mol Biol 18: 783788.
  • Watanabe, T.M., Tokuo, H., Gonda, K., Higuchi, H., and Ikebe, M. (2010) Myosin-X induces filopodia by multiple elongation mechanism. J Biol Chem 285: 1960519614.
  • Weber, K.L., Sokac, A.M., Berg, J.S., Cheney, R.E., and Bement, W.M. (2004) A microtubule-binding myosin required for nuclear anchoring and spindle assembly. Nature 431: 325329.
  • Wei, J., Goldberg, M.B., Burland, V., Venkatesan, M.M., Deng, W., Fournier, G., et al. (2003) Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun 71: 27752786.
  • Wei, Z., Yan, J., Lu, Q., Pan, L., and Zhang, M. (2011) Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain. Proc Natl Acad Sci USA 108: 35723577.
  • Zeile, W.L., Purich, D.L., and Southwick, F.S. (1996) Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actin-based Shigella motility. J Cell Biol 133: 4959.
  • Zhang, H., Berg, J.S., Li, Z., Wang, Y., Lang, P., Sousa, A.D., et al. (2004) Myosin-X provides a motor-based link between integrins and the cytoskeleton. Nat Cell Biol 6: 523531.