Interaction of Human Arp2/3 Complex and the Listeria monocytogenes ActA Protein in Actin Filament Nucleation-Reference-Cited by-同舟云学术

Interaction of Human Arp2/3 Complex and the Listeria monocytogenes ActA Protein in Actin Filament Nucleation

Published:1998-07-03 Issue:5373 Volume:281 Page:105-108
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Welch Matthew D.¹,Rosenblatt Jody¹,Skoble Justin¹,Portnoy Daniel A.¹,Mitchison Timothy J.¹

Affiliation:

1. M. D. Welch and J. Rosenblatt, Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA. T. J. Mitchison, Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. J. Skoble and D. A. Portnoy, Department of Molecular and Cell Biology and School of Public Health, University of California, Berkeley, CA 94720, USA.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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