Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation

被引：407

作者：

Welch, MD

Rosenblatt, J

Skoble, J

Portnoy, DA

Mitchison, TJ

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Univ Calif San Francisco, Dept Mol & Cellular Pharmacol, San Francisco, CA 94143 USA

[3] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

[4] Univ Calif Berkeley, Sch Publ Hlth, Berkeley, CA 94720 USA

来源：

SCIENCE | 1998年 / 281卷 / 5373期

关键词：

D O I：

10.1126/science.281.5373.105

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：

Actin filament assembly at the cell surface of the pathogenic bacterium Listeria monocytogenes requires the bacterial ActA surface protein and the host cell Arp2/3 complex. Purified Arp2/3 complex accelerated the nucleation of actin polymerization in vitro, but pure ActA had no effect. However, when combined, the Arp2/3 complex and ActA synergistically stimulated the nucleation of actin filaments. This mechanism of activating the host Arp2/3 complex at the L. monocytogenes surface may be similar to the strategy used by cells to control Arp2/3 complex activity and hence the spatial and temporal distribution of actin polymerization.

引用

页码：105 / 108

页数：4

共 42 条

[21] Cell motility driven by actin polymerization
Mogilner, A
Oster, G
[J]. BIOPHYSICAL JOURNAL, 1996, 71 (06) : 3030 - 3045
[22] The Saccharomyces cerevisiae actin-related protein arp2 is involved in the actin cytoskeleton
Moreau, V
Madania, A
Martin, RP
Winsor, B
[J]. JOURNAL OF CELL BIOLOGY, 1996, 134 (01) : 117 - 132
[23] ActA is a dimer
Mourrain, P
Lasa, I
Gautreau, A
Gouin, E
Pugsley, A
Cossart, P
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (19) : 10034 - 10039
[24] Arp2/3 complex from Acanthamoeba finds profilin and cross-links actin filaments
Mullins, RD
Kelleher, JF
Xu, J
Pollard, TD
[J]. MOLECULAR BIOLOGY OF THE CELL, 1998, 9 (04) : 841 - 852
[25] Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
Mullins, RD
Stafford, WF
Pollard, TD
[J]. JOURNAL OF CELL BIOLOGY, 1997, 136 (02) : 331 - 343
[26] THE BACTERIAL ACTIN NUCLEATOR PROTEIN ACTA OF LISTERIA-MONOCYTOGENES CONTAINS MULTIPLE BINDING-SITES FOR HOST MICROFILAMENT PROTEINS
PISTOR, S
CHAKRABORTY, T
WALTER, U
WEHLAND, J
[J]. CURRENT BIOLOGY, 1995, 5 (05) : 517 - 525
[27] THE PROLINE-RICH FOCAL ADHESION AND MICROFILAMENT PROTEIN VASP IS A LIGAND FOR PROFILINS
REINHARD, M
GIEHL, K
ABEL, K
HAFFNER, C
JARCHAU, T
HOPPE, V
JOCKUSCH, BM
WALTER, U
[J]. EMBO JOURNAL, 1995, 14 (08) : 1583 - 1589
[28] HOST-CELL ACTIN ASSEMBLY IS NECESSARY AND LIKELY TO PROVIDE THE PROPULSIVE FORCE FOR INTRACELLULAR MOVEMENT OF LISTERIA-MONOCYTOGENES
SANGER, JM
SANGER, JW
SOUTHWICK, FS
[J]. INFECTION AND IMMUNITY, 1992, 60 (09) : 3609 - 3619
[29] NEW YEAST ACTIN-LIKE GENE REQUIRED LATE IN THE CELL-CYCLE
SCHWOB, E
MARTIN, RP
[J]. NATURE, 1992, 355 (6356) : 179 - 182
[30] ASYMMETRIC DISTRIBUTION OF THE LISTERIA-MONOCYTOGENES ACTA PROTEIN IS REQUIRED AND SUFFICIENT TO DIRECT ACTIN-BASED MOTILITY
SMITH, GA
PORTNOY, DA
THERIOT, JA
[J]. MOLECULAR MICROBIOLOGY, 1995, 17 (05) : 945 - 951

← 1 2 3 4 5 →