title: 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.
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.
authors.affiliation: Institute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.
authors.forename: Carsten
authors.initials: C
authors.lastname: Schwan
authors.affiliation: Institute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany. klaus.aktories@pharmakol.uni-freiburg.de.
authors.forename: Klaus
authors.initials: K
authors.lastname: Aktories
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001427:Bacterial Toxins / Q000378:metabolism*; D048430:Cell Shape; D003013:Clostridium / Q000235:genetics / Q000378:metabolism*; D003015:Clostridium Infections / Q000378:metabolism* / Q000382:microbiology; D006801:Humans; D058105:Polymerization; D058112:Septins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D058112:Septins