The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins (original) (raw)
Loisel, T. P., Boujemaa, R., Pantaloni, D. & Carlier, M-F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature401, 613–616 (1999). ArticleCAS Google Scholar
Borisy, G. G. & Svitkina, T. M. Actin machinery: pushing the envelope. Curr. Opin. Cell Biol. (in the press).
Theriot, J. A. & Mitchison, T. J. Actin microfilament dynamics in locomoting cells. Nature352, 126– 131 (1991). ArticleCAS Google Scholar
Theriot, J. A., Mitchison, T. J., Tilney, L. G. & Portnoy, D. A. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature357, 257–260 (1992). ArticleCAS Google Scholar
Welch, M. D., Rosenblatt, J., Skoble, J., Portnoy, D. A. & Mitchison, T. J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science281, 105–108 ( 1998). ArticleCAS Google Scholar
Machesky, L. M. & Insall, R. H. Scar1 and the related Wiskott–Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol.8, 1347–1356 (1998). ArticleCAS Google Scholar
Machesky, L. M. et al. Scar, a WASp-related protein, activates dendritic nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA96, 3739–3744 (1999). ArticleCAS Google Scholar
Rohatgi, R. et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell97, 221–231 (1999). ArticleCAS Google Scholar
Yarar, D., To, W., Abo, A. & Welch, M. D. The Wiskott–Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol.9, 555–558 (1999). ArticleCAS Google Scholar
Winter, D., Lechler, T. & Li, R. Activation of the Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol.9, 501–504 ( 1999). ArticleCAS Google Scholar
Egile, C. et al. Activation of the Cdc42 effector N-WASP by the Shigella IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol.146, 1319 –1332 (1999). ArticleCAS Google Scholar
Small, J. V. Getting the actin filaments straight: nucleation–release or treadmilling Trends Cell Biol.5, 52–55 (1995). ArticleCAS Google Scholar
Carlier, M-F. Control of actin dynamics . Curr. Opin. Cell Biol.10, 45– 51 (1998). ArticleCAS Google Scholar
Svitkina, T. M. & Borisy, G. G. Arp2/3 complex and actin depolymerizing factor ADF/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol.145, 1009–1026 ( 1999). ArticleCAS Google Scholar
Mullins, R. D., Heuser, J. A. & Pollard, T. D. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping and formation of branched networks of filaments . Proc. Natl Acad. Sci. USA95, 6181– 6186 (1998). ArticleCAS Google Scholar
Higgs, H. N., Blanchoin, L. & Pollard, T. D. Influence of the C terminus of Wiskott–Aldrich Syndrome Protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry38, 15212–15222 (1999). ArticleCAS Google Scholar
Higgs, H. N. & Pollard, T. D. Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J. Biol. Chem.274, 32531–32534 ( 1999). ArticleCAS Google Scholar
Carlier, M-F., Pantaloni, D. & Korn, E. D. Polymerization of ADP–actin and ATP–actin under sonication and characteristics of the ATP–actin equilibrium polymer. J. Biol. Chem.260, 6565–6571.
Halsey, T. C. Diffusion-limited aggregation as branched growth. Phys. Rev. Lett.72, 1228–1231 ( 1994). ArticleCAS Google Scholar
Schafer, D. A. & Cooper, J. A. Control of actin assembly at filament ends. Annu. Rev. Cell Dev. Biol.11, 497–518 (1995). ArticleCAS Google Scholar
Sun, H. Q., Yamamoto, M., Mejillano, M. & Yin, H. L. Gelsolin, a multifunctional actin regulatory protein. J. Biol. Chem.274, 33179–33182 ( 1999). ArticleCAS Google Scholar
Laine, R. O. et al. Gelsolin, a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in host cells. Infect. Immun.66, 3775 –3782 (1998). CASPubMedPubMed Central Google Scholar
Cunningham, C., Stossel, T. P. & Kwiatkowski, D. Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin. Science251, 1233– 1236 (1991). ArticleCAS Google Scholar
Hug, C. et al. Capping protein levels influence actin assembly and cell motility in Dictyostelium. Cell81, 591– 600 (1995). ArticleCAS Google Scholar
Sun, H., Kwiatkowska, K., Wooten, D. & Yin, H. Effects of CapG overexpression on agonist-induced motility and second messenger generation . J. Cell Biol.129, 147– 156 (1995). ArticleCAS Google Scholar
Carlier, M.-F. & Pantaloni, D. Control of actin dynamics in cell motility. J. Mol. Biol.269, 459–467 (1997). ArticleCAS Google Scholar
Ressad, F., Didry, D., Egile, C., Pantaloni, D. & Carlier, M-F. Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and Arp2/3 complex J. Biol. Chem.274, 20970–20976 ( 1999). ArticleCAS Google Scholar
Carlier, M-F., Ressad, F. & Pantaloni, D. Control of actin dynamics in cell motility. Role of ADF/cofilin. J. Biol. Chem.274, 33827–33830 (1999). Article Google Scholar
Gouin, E. et al. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii. J. Cell Sci.112, 1697– 1708 (1999). CASPubMed Google Scholar
Huang, M. et al. Cdc42-induced actin filaments are protected from capping protein . Curr. Biol.9, 979–982 (1999). ArticleCAS Google Scholar
Kouyama, T. & Mihashi, K. Fluorimetry study of N-1-pyrenyl-iodoacetamide-labeled F-actin. Eur. J. Biochem.114, 33– 38 (1981). ArticleCAS Google Scholar
Pantaloni, D. & Carlier, M-F. How profilin promotes assembly of actin filaments in the presence of thymosin β4. Cell75, 1009 –1014 (1993). Article Google Scholar
Kuhlmann, P. A. & Fowler, V. M. Purification and characterization of an α1β2 isoform of CapZ from human erythrocytes: cytosolic location and inability to bind to Mg++ ghosts suggest that erythrocyte actin filaments are capped by adducin. Biochemistry36, 13461–13472 ( 1997). Article Google Scholar
Casella, J. F., Maack, D. J. & Lin, S. Purification and initial characterization of a protein from skeletal muscle that caps the barbed ends of actin filaments. J. Biol. Chem.261, 10915–10921 (1986). CASPubMed Google Scholar
Pollard, T. D. & Cooper, J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem.55, 987–1035 (1986). ArticleCAS Google Scholar
Laurent, V. et al. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes.J. Cell Biol.144, 1245–1258 (1999). ArticleCAS Google Scholar