Effects of ectopically expressed neuronal Wiskott-Aldrich syndrome protein domains on Rickettsia rickettsii actin-based motility

Infection and Immunity

Volumn 71, Issue 3, 2003, Pages 1551-1556

  Harlander, Ronald S ^a   Way, Michael ^b   Ren, Qun ^a   Howe, Dale ^a,c   Grieshaber, Scott S ^a,c   Heinzen, Robert A ^a,c  

^a UNIVERSITY OF WYOMING   (United States)

^b IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^c NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN;

ACTIN FILAMENT; ARTICLE; BLOOD VESSEL PERMEABILITY; CELL MOTILITY; CELL SPREADING; COMPLEX FORMATION; HUMAN; HUMAN CELL; LISTERIA MONOCYTOGENES; MOLECULAR INTERACTION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; RICKETTSIA RICKETTSII; WISKOTT ALDRICH SYNDROME;

ACTIN-RELATED PROTEIN 2; ACTIN-RELATED PROTEIN 3; CYTOSKELETAL PROTEINS; HELA CELLS; HUMANS; MOVEMENT; NERVE TISSUE PROTEINS; RICKETTSIA RICKETTSII; SHIGELLA FLEXNERI; STRUCTURE-ACTIVITY RELATIONSHIP; WISKOTT-ALDRICH SYNDROME PROTEIN, NEURONAL;

EID: 0037372690     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.3.1551-1556.2003     Document Type: Article

References (42)

1. Alrutz, M. A., A. Srivastava, K. W. Wong, C. D'Souza-Schorey, M. Tang, L. E. Ch'Ng, S. B. Snapper, and R. R. Isberg. 2001. Efficient uptake of Yersinia pseudotuberculosis via integrin receptors involves a Rac1-Arp 2/3 pathway that bypasses N-WASP function. Mol. Microbiol. 42:689-703.
2. Boujemaa-Paterski, R., E. Gouin, G. Hansen, S. Samarin, C. Le Clainche, D. Didry, P. Dehoux, P. Cossart, C. Kocks, M. F. Carlier, and D. Pantaloni. 2001. Listeria protein ActA mimics WASp family proteins: it activates filament barbed end branching by Arp2/3 complex. Biochemistry 40:11390-11404.
3. Caron, E. 2002. Regulation of Wiskott-Aldrich syndrome protein and related molecules. Curr. Opin. Cell. Biol. 14:82-87.
4. Cossart, P. 2000. Actin-based motility of pathogens: the Arp2/3 complex is a central player. Cell. Microbiol. 2:195-205.
5. Egile, C., T. P. Loisel, V. Laurent, R. Li, D. Pantaloni, P. J. Sansonetti, and M. F. Carlier. 1999. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146:1319-1332.
6. Elliott, D. A., D. J. Coleman, M. A. Lane, R. C. May, L. M. Machesky, and D. P. Clark. 2001. Cryptosporidium parvum infection requires host cell actin polymerization. Infect. Immun. 69:5940-5942.
7. Fradelizi, J., V. Nolreaux, J. Plastino, B. Menichi, D. Louvard, C. Sykes, R. M. Golsteyn, and E. Friederich. 2001. ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity. Nat. Cell Biol. 3:699-707.
8. Frischknecht, F., V. Moreau, S. Rottger, S. Gonfloni, I. Reckmann, G. Superti-Furga, and M. Way. 1999. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature 401:926-929.
9. Frischknecht, F., and M. Way. 2001. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11:30-38.
10. Goldberg, M. B. 2001. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65:595-626.
11. Gouin, E., H. Gantelet, C. Egile, I. Lasa, H. Ohayon, V. Villiers, P. Gounon, P. J. Sansonetti, and P. Cossart. 1999. A comparative study of the actinbased motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J. Cell Sci. 112:1697-1708.
12. Heinzen, R. A., S. S. Grieshaber, L. S. Van Kirk, and C. J. Devin. 1999. Dynamics of actin-based movement by Rickettsia rickettsii in Vero cells. Infect. Immun. 67:4201-4207.
13. Heinzen, R. A., S. F. Hayes, M. G. Peacock, and T. Hackstadt. 1993. Directional actin polymerization associated with spotted fever group rickettsia infection of Vero cells. Infect. Immun. 61:1926-1935.
14. Loisel, T. P., R. Boujemaa, D. Pantaloni, and M. F. Carlier. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401:613-616.
15. Lommel, S., S. Benesch, K. Rottner, T. Franz, J. Wehland, and R. Kuhn. 2001. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2:850-857.
16. Machesky, L. M., and K. L. Gould. 1999. The Arp2/3 complex: a multifunctional actin organizer. Curr. Opin. Cell Biol. 11:117-121.
17. Machesky, L. M., and R. H. Insall. 1998. Scarand the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347-1356.
18. Machesky, L. M., R. D. Mullins, H. N. Higgs, D. A. Kaiser, L. Blanchoin, R. C. May, M. E. Hall, and T. D. Pollard. 1999. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl. Acad. Sci. USA 96:3739-3744.
19. Martinez-Quiles, N., R. Rohatgi, I. M. Anton, M. Medina, S. P. Saville, H. Miki, H. Yamaguchi, T. Takenawa, J. H. Hartwig, R. S. Geha, and N. Ramesh. 2001. WIP regulates N-WASP-mediated actin polymerization and filopodium formation. Nat. Cell Biol. 3:484-491.
20. May, R. C., E. Caron, A. Hall, and L. M. Machesky. 2000. Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3. Nat. Cell Biol. 2:246-248.
21. May, R. C., M. E. Hall, H. N. Higgs, T. D. Pollard, T. Chakraborty, J. Wehland, L. M. Machesky, and A. S. Sechi. 1999. The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes. Curr. Biol. 9:759-762.
22. McGee, K., M. Zettl, M. Way, and M. Fallman. 2001. A role for N-WASP in invasin-promoted internalisation. FEBS Lett. 509:59-65.
23. Miki, H., K. Miura, and T. Takenawa. 1996. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15:5326-5335.
24. Miki, H., T. Sasaki, Y. Takai, and T. Takenawa. 1998. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391:93-96.
25. Mimuro, H., T. Suzuki, S. Suetsugu, H. Miki, T. Takenawa, and C. Sasakawa. 2000. Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri. J. Biol. Chem. 275:28893-28901.
26. Moreau, V., F. Frischknecht, I. Reckmann, R. Vincentelli, G. Rabut, D. Stewart, and M. Way. 2000. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell Biol. 2:441-448.
27. Mounier, J., V. Laurent, A. Hall, P. Fort, M. F. Carlier, P. J. Sansonetti, and C. Egile. 1999. Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell Sci. 112:2069-2080.
28. Mullins, R. D. 2000. How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures. Curr. Opin. Cell Biol. 12:91-96.
29. Mullins, R. D., J. A. Heuser, and T. D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95:6181-6186.
30. Pruyne, D., M. Evangelista, C. Yang, E. Bi, S. Zigmond, A. Bretscher, and C. Boone. 2002. Role of formins in actin assembly: nucleation and barbed-end association. Science 297:612-615.
31. Ramesh, N., I. M. Anton, J. H. Hartwig, and R. S. Geha. 1997. WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc. Natl. Acad. Sci. USA 94:14671-14676.
32. Rohatgi, R., H. Y. Ho, and M. W. Kirschner. 2000. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150:1299-1310.
33. Scaplehorn, N., A. Holmstrom, V. Moreau, F. Frischknecht, I. Reckmann, and M. Way. 2002. Grb2 and nck act cooperatively to promote actin-based motility of vaccinia virus. Curr. Biol. 12:740-745.
34. Shibata, T., F. Takeshima, F. Chen, F. W. Alt, and S. B. Snapper. 2002. Cdc42 facilitates invasion but not the actin-based motility of Shigella. Curr. Biol. 12:341-345.
35. Suzuki, T., H. Miki, T. Takenawa, and C. Sasakawa. 1998. Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17:2767-2776.
36. Teyssiere, N., C. Chiche-Portiche, and D. Raoult. 1992. Intracellular movements of Rickettsia conorii and R. typhi based on actin polymerization. Res. Microbiol. 143:821-829.
37. Van Kirk, L S., S. F. Hayes, and R. A. Heinzen. 2000. Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins. Infect. Immun. 68:4706-4713.
38. Welch, M. D., A. Iwamatsu, and T. J. Mitchison. 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:265-269.
39. Welch, M. O., J. Rosenblatt, J. Skoble, O. A. Portnoy, and T. J. Mitchison. 1998. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281:105-108.
40. Winkler, H. H. 1990. Rickettsia species (as organisms). Annu. Rev. Microbiol. 44:131-153.
41. Yamaguchi, H., H. Miki, S. Suetsugu, L. Ma, M. W. Kirschner, and T. Takenawa. 2000, Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP. Proc. Natl. Acad. Sci. USA 97:12631-12636.
42. Zeile, W. L., D. L. Purich, and F. S. Southwick. 1996. Recognition of two classes of oligoproline sequences in profilin-mediated acceleration of actinbased Shigella motility. J. Cell Biol. 133:49-59.