Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation.
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.
Welch
M D
MD
Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.
Rosenblatt
J
J
Skoble
J
J
Portnoy
D A
DA
Mitchison
T J
TJ
D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001704:Biopolymers; D002462:Cell Membrane / Q000378:metabolism; D015638:Cytochalasin D / Q000494:pharmacology; D003598:Cytoskeletal Proteins; D006801:Humans; D007700:Kinetics; D008089:Listeria monocytogenes / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008854:Microscopy, Electron
C495926:ACTR2 protein, human; C495928:ACTR3 protein, human; D051377:Actin-Related Protein 2; D051378:Actin-Related Protein 3; D000199:Actins; D001426:Bacterial Proteins; D001704:Biopolymers; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; C072980:actA protein, Listeria monocytogenes; D015638:Cytochalasin D