The actin cytoskeleton and bacterial infection. (2017)

• Record Type: Book
• Further Information: Note: Hans Georg Mannherz, editor.
• Editors: Mannherz, Hans Georg
• Contents: Preface; Contents; 45 Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins; Abstract; 1 Introduction; 2 Actin; 2.1 Actin Structure; 2.2 Binding Sites on Actin for Actin-Binding Proteins; 2.3 Filamentous (F- ) Actin; 2.4 Actin Dynamics: Polymerization Behaviour; 3 Interactions with Actin-Binding Proteins (ABPs); 3.1 G-actin-Sequestering Proteins; 3.2 F-actin-Nucleating Proteins and Their Nucleation-Promoting Factors (NPFs); 3.3 F-actin-Elongating Proteins; 3.4 F-actin-Capping Proteins; 3.5 F-actin-Bundling and Cross-linking Proteins; 3.6 F-actin-Stabilizing Proteins. 3.7 F-actin-Severing Proteins3.8 Regulation of the Activity and Localization of ABPs; 4 Examples of Bacterial Proteins that Subvert the Host Actin Cytoskeleton; 4.1 Direct Interactions of Bacterial Effectors with Actin; 4.1.1 Direct Modifications of G-actin; 4.1.2 F-actin Dynamics Modifying Bacterial Proteins; 4.2 Manipulation of Actin-Binding Proteins by Bacterial Effectors; 4.2.1 Recruitment and Regulation of the Host F-actin Nucleation Machinery; 4.2.2 Interactions of Bacterial Effectors with Actin-Binding Proteins (ABPs). 4.2.3 Manipulation of Host ABP Regulation: Rho GTPases, Kinases, and Phospholipids as Bacterial Targets5 Conclusions; References; 25 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; 1 Introduction; 2 Actin-Depolymerizing Toxins; 2.1 Structure of Binary Toxins; 2.2 Receptors and Uptake; 3 Modification of Actin by ADP-Ribosylating Toxins; 4 Cellular Consequences of the ADP-Ribosylation of Actin in Arginine-177. 4.1 Effects of Actin-Depolymerizing Toxins on Microtubules4.2 Mechanisms Involved in Protrusion Formation: A Role for Septins; 4.3 Role and Functions of Toxin-Induced Cell Protrusions; 4.3.1 Re-guidance of Vesicle Traffic; 5 Conclusions; References; 43 Photorhabdus luminescens Toxins TccC3 and TccC5 Affect the Interaction of Actin with Actin-Binding Proteins Essential for Treadmilling; Abstract; 1 Introduction; 2 Life Cycle and Tc Toxins of Photorhabdus luminescens; 3 ADP-Ribosylation of Actin by P. luminescens TccC3; 3.1 Thr148-ADP-Ribosylation Promotes Actin Polymerization. 3.2 Impaired Interactions of Thr148-ADP-Ribosylated Actin with a Number of Actin-Binding Proteins4 ADP-Ribosylation of Rho GTPases by Photorhabdus luminescens TccC5; 5 Conclusions; References; 23 Comparative Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins: Insight from Structural Biology; Abstract; 1 Introduction; 2 Functional and Structural Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins; 3 Comparative Studies of Substrate Recognition by Actin- and Rho-Specific ARTs; 4 Cell Entry Mechanism Between Actin- and Rho-Specific ARTs; 5 Conclusion; Acknowledgements; References.
• Publisher Details: Cham, Switzerland : Springer
• Publication Date: 2017
• Extent: 1 online resource (x, 242 pages), illustrations
• Subjects: 572/.66; 610; Medicine; Actin; Cytoskeleton; SCIENCE -- Life Sciences -- Biochemistry; Actin; Cytoskeleton; Bacteria -- metabolism; Bacterial Infections -- metabolism; Actin Cytoskeleton; Medical -- Pharmacology; Pharmacology; Microbiology; Toxicology; Medical -- Microbiology; Medical microbiology & virology; Electronic books
• Languages: English
• ISBNs: 9783319500478; 3319500473
• Related ISBNs: 9783319500461; 3319500465
• Notes: Note: Online resource; title from PDF title page (SpringerLink, viewed February 16, 2017).
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.