Purification and architecture of the ubiquitous Wave complex

被引:192
作者
Gautreau, A [1 ]
Ho, HYH [1 ]
Li, JX [1 ]
Steen, H [1 ]
Gygi, SP [1 ]
Kirschner, MW [1 ]
机构
[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
关键词
D O I
10.1073/pnas.0400628101
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The Wave proteins are major activators of the Arp2/3 complex. The ubiquitous Wave-2 is required for actin polymerization at the leading edge of migrating cells. Here we purify Wave-2 from HeLa cells. Five proteins, Sra, Nap, Wave-2, Abi, and Hspc, are copurified, indicating that they form a tight complex. These proteins are only present in the complexed form, with the exception of Hspc, which displays a free pool. We reconstitute the Wave-2 complex by cotranslating in vitro the five subunits and use this system together with specific immunoprecipitations to study the molecular architecture of the complex. The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.
引用
收藏
页码:4379 / 4383
页数:5
相关论文
共 23 条
[1]   PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium [J].
Blagg, SL ;
Stewart, M ;
Sambles, C ;
Insall, RH .
CURRENT BIOLOGY, 2003, 13 (17) :1480-1487
[2]   Kette regulates actin dynamics and genetically interacts with Wave and Wasp [J].
Bogdan, S ;
Klämbt, C .
DEVELOPMENT, 2003, 130 (18) :4427-4437
[3]   Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck [J].
Eden, S ;
Rohatgi, R ;
Podtelejnikov, AV ;
Mann, M ;
Kirschner, MW .
NATURE, 2002, 418 (6899) :790-793
[4]   Rho GTPases in cell biology [J].
Etienne-Manneville, S ;
Hall, A .
NATURE, 2002, 420 (6916) :629-635
[5]   Correlation between protein and mRNA abundance in yeast [J].
Gygi, SP ;
Rochon, Y ;
Franza, BR ;
Aebersold, R .
MOLECULAR AND CELLULAR BIOLOGY, 1999, 19 (03) :1720-1730
[6]   Scar/WAVE is localised at the tips of protruding lamellipodia in living cells [J].
Hahne, P ;
Sechi, A ;
Benesch, S ;
Small, JV .
FEBS LETTERS, 2001, 492 (03) :215-220
[7]   Molecular cloning of p125(Nap1), a protein that associates with an SH3 domain of Nck [J].
Kitamura, T ;
Kitamura, Y ;
Yonezawa, K ;
Totty, NF ;
Gout, I ;
Hara, K ;
Waterfield, MD ;
Sakaue, M ;
Ogawa, W ;
Kasuga, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1996, 219 (02) :509-514
[8]   p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase [J].
Kobayashi, K ;
Kuroda, S ;
Fukata, M ;
Nakamura, T ;
Nagase, T ;
Nomura, N ;
Matsuura, Y ;
Yoshida-Kubomura, N ;
Iwamatsu, A ;
Kaibuchi, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (01) :291-295
[9]   Abi, Sra1, and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions [J].
Kunda, P ;
Craig, G ;
Dominguez, V ;
Baum, B .
CURRENT BIOLOGY, 2003, 13 (21) :1867-1875
[10]   Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells [J].
Lommel, S ;
Benesch, S ;
Rottner, K ;
Franz, T ;
Wehland, J ;
Kühn, R .
EMBO REPORTS, 2001, 2 (09) :850-857