The actin cytoskeleton and bacterial infection /
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| Imprint: | Cham, Switzerland : Springer, 2017. |
|---|---|
| Description: | 1 online resource (x, 242 pages) : illustrations |
| Language: | English |
| Series: | Current topics in microbiology and immunology, 0070-217X ; volume 399 Current topics in microbiology and immunology ; v. 399. |
| Subject: | |
| Format: | E-Resource Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/11271586 |
Table of 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.