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Control of actin turnover by a salmonella invasion protein.

McGhie, EJ; Hayward, RD; Koronakis, V; (2004) Control of actin turnover by a salmonella invasion protein. Mol Cell , 13 (4) pp. 497-510. 10.1016/S1097-2765(04)00053-X. Green open access

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Abstract

Salmonella force their way into nonphagocytic host intestinal cells to initiate infection. Uptake is triggered by delivery into the target cell of bacterial effector proteins that stimulate cytoskeletal rearrangements and membrane ruffling. The Salmonella invasion protein A (SipA) effector is an actin binding protein that enhances uptake efficiency by promoting actin polymerization. SipA-bound actin filaments (F-actin) are also resistant to artificial disassembly in vitro. Using biochemical assays of actin dynamics and actin-based motility models, we demonstrate that SipA directly arrests cellular mechanisms of actin turnover. SipA inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. SipA also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments. These data suggest that SipA focuses host cytoskeletal reorganization by locally inhibiting both ADF/cofilin- and gelsolin-directed actin disassembly, while simultaneously stimulating pathogen-induced actin polymerization.

Type: Article
Title: Control of actin turnover by a salmonella invasion protein.
Location: United States
Open access status: An open access version is available from UCL Discovery
DOI: 10.1016/S1097-2765(04)00053-X
Publisher version: https://doi.org/10.1016/S1097-2765(04)00053-X
Language: English
Additional information: Copyright © 2004 Cell Press. All rights reserved. Articles published under an Elsevier user license are protected by copyright and may be used for non-commercial purposes. Users may access, download, copy, translate, text mine and data mine the articles.
Keywords: Actin Depolymerizing Factors, Actins, Animals, Bacterial Proteins, Binding Sites, Cell Extracts, Cytoskeleton, Destrin, Gelsolin, Host-Parasite Interactions, Microfilament Proteins, Models, Molecular, Protein Structure, Tertiary, Recombinant Proteins, Salmonella, Xenopus
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
URI: https://discovery.ucl.ac.uk/id/eprint/76183
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