Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function

Journal of Cell Biology

Volumn 168, Issue 2, 2005, Pages 315-328

  Martin, Adam C ^a   Xu, Xiao Ping ^b   Rouiller, Isabelle ^b   Kaksonen, Marko ^a   Sun, Yidi ^a   Belmont, Lisa ^c   Volkmann, Niels ^b   Hanein, Dorit ^b   Welch, Matthew ^a   Drubin, David G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b BURNHAM INSTITUTE   (United States)

^c Cytokinetics Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; NUCLEOTIDE BINDING PROTEIN;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CYTOARCHITECTURE; CYTOSKELETON; ELECTRON MICROSCOPY; ENDOCYTOSIS; GENE MUTATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

ACTIN-RELATED PROTEIN 2; ACTIN-RELATED PROTEIN 3; ACTINS; ADENOSINE TRIPHOSPHATE; BINDING SITES; CARRIER PROTEINS; CYTOSKELETAL PROTEINS; CYTOSKELETON; ENDOCYTOSIS; GREEN FLUORESCENT PROTEINS; IMAGE PROCESSING, COMPUTER-ASSISTED; ISOQUINOLINES; MICROFILAMENT PROTEINS; MICROSCOPY, ELECTRON; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; NUCLEOTIDES; PHENOTYPE; POLYMERS; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUPPRESSION, GENETIC; WISKOTT-ALDRICH SYNDROME PROTEIN;

EID: 13844250532     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200408177     Document Type: Article

References (44)

1. Amann, K.J., and T.D. Pollard. 2001. The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat. Cell Biol. 3:306-310.
2. Belmont, L.D., and D.G. Drubin. 1998. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142:1289-1299.
3. Belmont, L.D., A. Orlova, D.G. Drubin, and E.H. Egelman. 1999a. A change in actin conformation associated with filament instability after Pi release. Proc. Natl. Acad. Sci. USA. 96:29-34.
4. Belmont, L.D., G.M. Patterson, and D.G. Drubin. 1999b. New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J. Cell Sci. 112(Pt 9):1325-1336.
5. Bernheim-Groswasser, A., S. Wiesner, R.M. Golsteyn, M.F. Carlier, and C. Sykes. 2002. The dynamics of actin-based motility depend on surface parameters. Nature. 417:308-311.
6. Blanchoin, L., K.J. Amann, H.N. Higgs, J.B. Marchand, D.A. Kaiser, and T.D. Pollard. 2000. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature. 404:1007-1011.
7. Chen, X., J. Peng, M. Pedram, C.A. Swenson, and P.A. Rubenstein. 1995. The effect of the S14A mutation on the conformation and thermostability of Saccharomyces cerevisiae G-actin and its interaction with adenine nucleotides. J. Biol. Chem. 270:11415-11423.
8. Dayel, M.J., and R.D. Mullins. 2004. Activation of Arp2/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2. PLoS Biol 2:E91.
9. Dayel, M.J., E.A. Holleran, and R.D. Mullins. 2001. Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments. Proc. Natl. Acad. Sci. USA. 98:14871-14876.
10. Duncan, M.C., M.J. Cope, B.L. Goode, B. Wendland, and D.G. Drubin. 2001. Yeast Eps15-like endocytic protein, Panlp, activates the Arp2/3 complex. Nat. Cell Biol. 3:687-690.
11. Engqvist-Goldstein, A.E., and D.G. Drubin. 2003. Actin assembly and endocytosis: from yeast to mammals. Annu. Rev. Cell Dev. Biol. 19:287-332.
12. Goley, E.D., S.E. Rodenbusch, A.C. Martin, and M.D. Welch. 2004. Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell. 16:269-279.
13. Higgs, H.N., L. Blanchoin, and T.D. Pollard. 1999. Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry. 38:15212-15222.
14. Jonsdottir, G.A., and R. Li. 2004. Dynamics of yeast Myosin I: evidence for a possible role in scission of endocytic vesicles. Curr. Biol. 14:1604-1609.
15. Kabsch, W., H.G. Mannherz, D. Suck, E.F. Pai, and K.C. Holmes. 1990. Atomic structure of the actin:DNase I complex. Nature. 347:37-44.
16. Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell. 115:475-487.
17. Lasa, I., E. Gouin, M. Goethals, K. Vancompernolle, V. David, J. Vandekerckhove, and P. Cossart. 1997. Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes. EMBO J. 16:1531-1540.
18. Le Clainche, C., D. Didry, M.F. Carlier, and D. Pantaloni. 2001. Activation of Arp2/3 complex by Wiskott-Aldrich syndrome protein is linked to enhanced binding of ATP to Arp2. J. Biol. Chem. 276:46689-46692.
19. Le Clainche, C., D. Pantaloni, and M.F. Carlier. 2003. ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays. Proc. Natl. Acad. Sci. USA. 100:6337-6342.
20. Ludtke, S.J., P.R. Baldwin, and W. Chiu. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97.
21. Madania, A., P. Dumoulin, S. Grava, H. Kitamoto, C. Scharer-Brodbeck, A. Soulard, V. Moreau, and B. Winsor. 1999. The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol. Biol. Cell. 10:3521-3538.
22. Marchand, J.B., D.A. Kaiser, T.D. Pollard, and H.N. Higgs. 2001. Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nat. Cell Biol. 3:76-82.
23. Merrifield, C.J., M.E. Feldman, L. Wan, and W. Almers. 2002. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4:691-698.
24. Merrifield, C.J., B. Qualmann, M.M. Kessels, and W. Aimers. 2004. Neural Wiskott-Aldrich syndrome protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts. Eur. J. Cell Biol. 83:13-18.
25. Moreau, V., A. Madania, R.P. Martin, and B. Winsor. 1996. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134:117-132.
26. Moreau, V., J.M. Galan, G. Devilliers, R. Haguenauer-Tsapis, and B. Winsor. 1997. The yeast actin-related protein Arp2p is required for the internalization step of endocytosis. Mol. Biol. Cell. 8:1361-1375.
27. Pan, F., C. Egile, T. Lipkin, and R. Li. 2004. ARPC1/Arc40 mediates the interaction of the Arp2/3 complex with WASP family activators. J. Biol. Chem. 279:54629-54636.
28. Panchal, S.C., D.A. Kaiser, E. Torres, T.D. Pollard, and M.K. Rosen. 2003. A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nat. Struct. Biol. 10:591-598.
29. Robinson, R.C., K. Turbedsky, D.A. Kaiser, J.B. Marchand, H.N. Higgs, S. Choe, and T.D. Pollard. 2001. Crystal structure of Arp2/3 complex. Science. 294:1679-1684.
30. Rodal, A.A., A.L. Manning, B.L. Goode, and D.G. Drubin. 2003. Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr. Biol. 13:1000-1008.
31. Sablin, E.P., J.F. Dawson, M.S. VanLoock, J.A. Spudich, E.H. Egelman, and R.J. Fletterick. 2002. How does ATP hydrolysis control actin's associations? Proc. Natl. Acad. Sci. USA. 99:10945-10947.
32. Skoble, J., D.A. Portnoy, and M.D. Welch. 2000. Three regions within ActA promote Arp2/3 complex-mediated actin nucleation and Listeria monocytogenes motility. J. Cell Biol. 150:527-538.
33. Svitkina, T.M., and G.G. Borisy. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-1026.
34. Volkmann, N., and D. Hanein. 1999. Quantitative fitting of atomic models into observed densities derived by electron microscopy. J. Struct. Biol. 125:176-184.
35. Volkmann, N., and D. Hanein. 2003. Docking of atomic models into reconstructions from electron microscopy. Methods Enzymol. 374:204-225.
36. Volkmann, N., K.J. Amann, S. Stoilova-McPhie, C. Egile, D.C. Winter, L. Hazelwood, J.E. Heuser, R. Li, T.D. Pollard, and D. Hanein. 2001. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science. 293:2456-2459.
37. Vorobiev, S., B. Strokopytov, D.G. Drubin, C. Frieden, S. Ono, J. Condeelis, P.A. Rubenstein, and S.C. Almo. 2003. The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proc. Natl. Acad. Sci. USA. 100:5760-5765.
38. Welch, M.D., and R.D. Mullins. 2002. Cellular control of actin nucleation. Annu. Rev. Cell Dev. Biol. 18:247-288.
39. Wen, K.K., X. Yao, and P.A. Rubenstein. 2002. GTP-yeast actin. J. Biol. Chem. 277:41101-41109.
40. Wertman, K.F., D.G. Drubin, and D. Botstein. 1992. Systematic mutational analysis of the yeast ACT1 gene. Genetics. 132:337-350.
41. Winter, D., A.V. Podtelejnikov, M. Mann, and R. Li. 1997. The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr. Biol. 7:519-529.
42. Winter, D.C., E.Y. Choe, and R. Li. 1999. Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc. Natl. Acad. Sci. USA. 96:7288-7293.
43. Wolven, A.K., L.D. Belmont, N.M. Mahoney, S.C. Almo, and D.G. Drubin. 2000. In vivo importance of actin nucleotide exchange catalyzed by profilin. J. Cell Biol. 150:895-904.
44. Young, M.E., J.A. Cooper, and P.C. Bridgman. 2004. Yeast actin patches are networks of branched actin filaments. J. Cell Biol. 166:629-635.