Signalling to actin: The Cdc42-N-WASP-Arp2/3 connection

Chemistry and Biology

Volumn 6, Issue 9, 1999, Pages

  Carlier, Marie France ^a   Ducruix, Arnaud ^a,b   Pantaloni, Dominique ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033200370     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80107-0     Document Type: Review

References (28)

1. Welch, M.D., Iwamatsu, A. & Mitchison, T.J. (1997). Actin polymerization is induced by the Arp2/3 complex at the surface of Listeria monocytogenes. Nature 385, 265-269.
2. Welch, M.D., Rosenblatt, J., Skoble, J., Portnoy, D.A. & Mitchison, T.J. (1998). Interaction of human Arp2/3 complex and the Listeria monocytogenes actA protein in actin filament nucleation. Science 281, 105-108.
3. Zigmond, S.H. (1998). Actin cytoskeleton: The Arp2/3 complex gets to the point. Curr. Biol. 8, R654-R657.
4. Mullins, R.D., Heuser, J.A. & Pollard, T.D. (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.
5. Sritkina, T.M. & Borisy, G.G. (1999). Arp2/3 complex and actin depolimerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell. Biol. 145, 1009-1026.
6. Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
7. Aspenström, P., Lindberg, U. & Hall, A. (1996). Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr. Biol. 6, 70-75.
8. Symons, M., et al., & Abo, A. (1996). Wiskott-Aldrich syndrome protein, a novel effector of the GTPase Cdc42Hs, is implicated in actin polymerization. Cell 84, 723-734.
9. Kolluri, R.S., Tolias, K.F., Carpenter, C.L., Rosen, F.S. & Kirchhausen, T. (1996). Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42. Proc. Natl Acad. Sci. USA 93, 5615-5618.
10. Li, R. (1997). Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136, 649-658.
11. Bear, J.E., Rawls, J.F. & Saxe, C.L. (1998). SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development. J. Cell Biol. 142, 1325-1335.
12. Miki, H., Sasaki, T., Takai, Y. & Takenawa, T. (1998). Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391, 93-96.
13. Prehoda, K.E., Lee, O.J., & Lim, W.A. (1999). Structure of an enabled/VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly. Cell 97, 471-480.
14. Zigmond, S.H., Joyce, M., Yang, C., Brown, K., Huang, M. & Pring, M. (1998) Mechanism of Cdc42-induced actin polymerization in neutrophil extracts. J. Cell Biol. 142, 1001-1012.
15. Ma, L., Rohatgi, R. & Kirschner, M.W. (1998) The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc. Natl Acad. Sci. USA 95, 15362-15367.
16. Machesky, L.M. & Insall, R.H. (1998). Scar1 and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356.
17. Machesky, L.M., et al., & Pollard, T.D. (1999). Scar, a WASP-related protein, activates dendritic nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA 96, 3739-3744.
18. Rohatgi, R., et al., & Kirschner, M.W. (1999). The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231.
19. Suzuki, T., Miki, H., Takenawa, T. & Sasakawa, C. (1998). Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17, 2767-2776.
20. Yarar, D., To, W., Abo, A. & Welch, M.D. (1999). The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9, 555-558.
21. Winter, D., Lechler, T. & Li, R. (1999). Activation of the yeast Arp2/3 complex by Bee1 p, a WASP-family protein. Curr. Biol. 9, 501-504.
22. Abdul-Manan, N., et al., & Rosen, M.K. (1999). Solution structure of Cdc42 in complex with the GTPase binding domain of the Wiskott-Aldrich syndrome protein. Nature 399, 379-383.
23. Rudolph, M.G., Bayer, P., Abo, A., Kuhlmann, J., Vetter, I.R. & Wittinghofer, A. (1998). The Cdc42/Rac interactive binding region motif of the Wiskott-Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. J. Biol. Chem. 273, 18067-18076.
24. Nassar, N., Horn, G., Herrmann, C., Block, C., Janknecht, R. & Wittinghofer, A. (1996). Ras/Rap effector specificity determined by charge reversal. Nat. Struct. Biol. 3, 723-729.
25. Leonard, D.A., Satoskar, R.S., Wu, W.-J., Bagrodia, S., Cerione, R.A. & Manor, D. (1997). Use of a fluorescence spectroscopic readout to characterize the interactions of Cdc42Hs with its target effector, mPAK-3. Biochemistry 36, 1173-1180.
26. Verkhovsky A.B., Svitkina T.M. & Borisy G.G. (1999). Self-polarization and directional motility of cytoplasm. Curr. Biol. 9, 11-20.
27. Sells, M.A., Knaus, U.G., Bagrodia, S., Ambrose, D.M., Bokoch, G.M. & Chernoff, J. (1997). Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells. Curr. Biol. 7, 202-210.
28. Machesky, L.M. (1997). Cell motility: Complex dynamics at the leading edge. Curr. Biol., 7, R164-R167.