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 |
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| 245 | 0 | 4 | |a The actin cytoskeleton and bacterial infection / |c Hans Georg Mannherz, editor. |
| 264 | 1 | |a Cham, Switzerland : |b Springer, |c 2017. | |
| 300 | |a 1 online resource (x, 242 pages) : |b illustrations | ||
| 336 | |a text |b txt |2 rdacontent | ||
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| 347 | |a text file | ||
| 347 | |b PDF | ||
| 490 | 1 | |a Current topics in microbiology and immunology, |x 0070-217X ; |v volume 399 | |
| 505 | 0 | |a 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. | |
| 505 | 8 | |a 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). | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 505 | 8 | |a 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. | |
| 588 | 0 | |a Online resource; title from PDF title page (SpringerLink, viewed February 16, 2017). | |
| 520 | |a This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton of host cells. Bacteria have developed a veritable arsenal of toxins, effector proteins and virulence factors that allow them to modify the properties of the intracellular actin cytoskeleton for their own purposes. Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton. In short, this volume provides an overview of the various tricks bacteria have evolved to ℓ́ℓact on actinℓ́ℓ in order to hijack this essential host cell component for their own needs. As such, it will be of interest to scientists from many fields, as well as clinicians whose work involves infectious diseases. | ||
| 650 | 0 | |a Actin. |0 http://id.loc.gov/authorities/subjects/sh85000687 | |
| 650 | 0 | |a Cytoskeleton. |0 http://id.loc.gov/authorities/subjects/sh85035256 | |
| 650 | 2 | |a Bacteria |x metabolism. | |
| 650 | 2 | |a Bacterial Infections |x metabolism. | |
| 650 | 2 | |a Actin Cytoskeleton. | |
| 650 | 7 | |a Pharmacology. |2 bicssc | |
| 650 | 7 | |a Medical microbiology & virology. |2 bicssc | |
| 650 | 7 | |a SCIENCE |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Actin. |2 fast |0 (OCoLC)fst00796140 | |
| 650 | 7 | |a Cytoskeleton. |2 fast |0 (OCoLC)fst00886325 | |
| 655 | 4 | |a Electronic books. | |
| 700 | 1 | |a Mannherz, Hans Georg, |e editor. |0 http://id.loc.gov/authorities/names/nb2017005983 | |
| 776 | 0 | 8 | |i Print version: |t Actin cytoskeleton and bacterial infection. |d Cham, Switzerland : Springer, 2017 |z 3319500465 |z 9783319500461 |w (OCoLC)962005647 |
| 830 | 0 | |a Current topics in microbiology and immunology ; |v v. 399. |0 http://id.loc.gov/authorities/names/n42036058 | |
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