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Cited by 522

The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

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

Open access
Egile, Coumaran, Loisel, Thomas P., Laurent, Valérie, Li, Rong, Pantaloni, Dominique, Sansonetti, Philippe J., Carlier, Marie-France·1999·The Journal of Cell Biology
DOI 10.1083/jcb.146.6.1319
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Abstract

To propel itself in infected cells, the pathogen Shigella flexneri subverts the Cdc42-controlled machinery responsible for actin assembly during filopodia formation. Using a combination of bacterial motility assays in platelet extracts with Escherichia coli expressing the Shigella IcsA protein and in vitro analysis of reconstituted systems from purified proteins, we show here that the bacterial protein IcsA binds N-WASP and activates it in a Cdc42-like fashion. Dramatic stimulation of actin assembly is linked to the formation of a ternary IcsA–N-WASP–Arp2/3 complex, which nucleates actin polymerization. The Arp2/3 complex is essential in initiation of actin assembly and Shigella movement, as previously observed for Listeria monocytogenes. Activation of N-WASP by IcsA unmasks two domains acting together in insertional actin polymerization. The isolated COOH-terminal domain of N-WASP containing a verprolin-homology region, a cofilin-homology sequence, and an acidic terminal segment (VCA) interacts with G-actin in a unique profilin-like functional fashion. Hence, when N-WASP is activated, its COOH-terminal domain feeds barbed end growth of filaments and lowers the critical concentration at the bacterial surface. On the other hand, the NH2-terminal domain of N-WASP interacts with F-actin, mediating the attachment of the actin tail to the bacterium surface. VASP is not involved in Shigella movement, and the function of profilin does not require its binding to proline-rich regions.

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Metadata

Authors
Egile, C., Loisel, T. P., Laurent, V., Li, R., Pantaloni, D., Sansonetti, P. J., & Carlier, M.-F.
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
1999-09-20
Volume
146
Issue
6
Pages
1319-1332
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.146.6.1319
OpenAlex
W2148334175
Cited by
522
References
51
FWCI
22.65
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: 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. https://app.cochat.ai/papers/10.1083/jcb.146.6.1319
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Egile, C., Loisel, T. P., Laurent, V., Li, R., Pantaloni, D., Sansonetti, P. J., & Carlier, M.-F. (1999). 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. The Journal of Cell Biology. https://doi.org/10.1083/jcb.146.6.1319

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