The dynamics of actin-based motility depend on surface parameters

被引:193
作者
Bernheim-Groswasser, A
Wiesner, S
Golsteyn, RM
Carlier, MF
Sykes, C
机构
[1] Inst Curie, Lab Physicochim Curie, CNRS, UMR 168, F-75231 Paris 05, France
[2] Lab Enzymol & Biochim Struct, CNRS, UPR A 9063, F-91198 Gif Sur Yvette, France
关键词
D O I
10.1038/417308a
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
In cells, actin polymerization at the plasma membrane is induced by the recruitment of proteins such as the Arp2/3 complex, and the zyxin/VASP complex(1-3). The physical mechanism of force generation by actin polymerization has been described theoretically using various approaches(4-6), but lacks support from experimental data. By the use of reconstituted motility medium 7,we find that the Wiskott-Aldrich syndrome protein(8,9) (WASP) subdomain, known as VCA, is sufficient to induce actin polymerization and movement when grafted on microspheres. Changes in the surface density of VCA protein or in the microsphere diameter markedly affect the velocity regime, shifting from a continuous to a jerky movement resembling that of the mutated 'hopping' Listeria(10). These results highlight how simple physical parameters such as surface geometry and protein density directly affect spatially controlled actin polymerization, and play a fundamental role in actin-dependent movement.
引用
收藏
页码:308 / 311
页数:4
相关论文
共 29 条
[1]   Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts [J].
Beningo, KA ;
Dembo, M ;
Kaverina, I ;
Small, JV ;
Wang, YL .
JOURNAL OF CELL BIOLOGY, 2001, 153 (04) :881-887
[2]   Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins [J].
Blanchoin, L ;
Amann, KJ ;
Higgs, HN ;
Marchand, JB ;
Kaiser, DA ;
Pollard, TD .
NATURE, 2000, 404 (6781) :1007-1011
[3]   Motility of ActA protein-coated microspheres driven by actin polymerization [J].
Cameron, LA ;
Footer, MJ ;
van Oudenaarden, A ;
Theriot, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (09) :4908-4913
[4]   Dendritic organization of actin comet tails [J].
Cameron, LA ;
Svitkina, TM ;
Vignjevic, D ;
Theriot, JA ;
Borisy, GG .
CURRENT BIOLOGY, 2001, 11 (02) :130-135
[5]   Growth of branched actin networks against obstacles [J].
Carlsson, AE .
BIOPHYSICAL JOURNAL, 2001, 81 (04) :1907-1923
[6]   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].
Egile, C ;
Loisel, TP ;
Laurent, V ;
Li, R ;
Pantaloni, D ;
Sansonetti, PJ ;
Carlier, MF .
JOURNAL OF CELL BIOLOGY, 1999, 146 (06) :1319-1332
[7]   ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity [J].
Fradelizi, J ;
Noireaux, V ;
Plastino, J ;
Menichi, B ;
Louvard, D ;
Sykes, C ;
Golsteyn, RM ;
Friederich, E .
NATURE CELL BIOLOGY, 2001, 3 (08) :699-707
[8]   An elastic analysis of Listeria monocytogenes propulsion [J].
Gerbal, F ;
Chaikin, P ;
Rabin, Y ;
Prost, J .
BIOPHYSICAL JOURNAL, 2000, 79 (05) :2259-2275
[9]   On the 'Listeria' propulsion mechanism [J].
Gerbal, F ;
Noireaux, V ;
Sykes, C ;
Jülicher, F ;
Chaikin, P ;
Ott, A ;
Prost, J ;
Golsteyn, RM ;
Friederich, E ;
Louvard, D ;
Laurent, V ;
Carlier, MF .
PRAMANA-JOURNAL OF PHYSICS, 1999, 53 (01) :155-170
[10]   Effects of intermediate filaments on actin-based motility of Listeria monocytogenes [J].
Giardini, PA ;
Theriot, JA .
BIOPHYSICAL JOURNAL, 2001, 81 (06) :3193-3203