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Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins

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The Actin Cytoskeleton and Bacterial Infection

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 399))

Abstract

A large group of bacterial protein toxins, including binary ADP-ribosylating toxins, modify actin at arginine-177, thereby actin polymerization is blocked and the actin cytoskeleton is redistributed. Modulation of actin functions largely affects other components of the cytoskeleton, especially microtubules and septins. Here, recent findings about the functional interconnections of the actin cytoskeleton with microtubules and septins, affected by bacterial toxins, are reviewed.

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Authors and Affiliations

  1. Institute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany

    Carsten Schwan & Klaus Aktories

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  1. Carsten Schwan
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  2. Klaus Aktories
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Correspondence to Klaus Aktories .

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  1. Institut für Anatomie, Abteilung für Anatomie und Molekulare Embryologie, Ruhr-Universität Bochum, Bochum, Germany

    Hans Georg Mannherz

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Schwan, C., Aktories, K. (2016). Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins. In: Mannherz, H. (eds) The Actin Cytoskeleton and Bacterial Infection. Current Topics in Microbiology and Immunology, vol 399. Springer, Cham. https://doi.org/10.1007/82_2016_25

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