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Molecular biology of arrestins /
This special volume of Progress in Molecular Biology and Translational Science focuses on the molecular biology of arrestins, with contributions from leaders in the field. Arrestins have emerged as central players in the regulation of many facets of G protein-coupled receptor signaling. This volume...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Elsevier Science & Technology,
2013.
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| Colección: | Progress in molecular biology and translational science ;
v. 118. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- Front Cover; The Molecular Biology of Arrestins; Copyright; Contents; Contributors; Preface; Part I: Perspective-The Duality of Arrestin Function; Chapter One: Arrestins Come of Age: A Personal Historical Perspective; 1. Introduction; 2. ��Prehistory�� of Arrestins; 3. A Family of 7 Transmembrane Receptors; 4. The GRK and Arrestin Families; 5. Arrestins and Desensitization; 6. Arrestins and Endocytosis; 7. Arrestins and Signaling; 8. Biased Signaling; 9. Bar Code Hypothesis; 10. Other Receptors, Other Functions; 11. Future Perspectives; References; Part II: The Molecular Biology of Arrestins.
- Chapter Two: True Arrestins and Arrestin-Fold Proteins: A Structure-Based Appraisal1. Introduction; 2. True Arrestins: A Structure Adapted to Multiple Scaffolding; 2.1. Function of arrestins; 2.2. Crystal structure of arrestins; 2.3. Binding sites for the endocytic machinery on arrestin�s C-terminal tail; 2.4. Sites of posttranslational modifications; 2.5. Binding sites for inositol phosphates; 2.6. Conservation analysis of essential residues among visual and �-arrestins; 3. Novel Arrestin-Related Proteins; 3.1. Mammalian ARRDCs; 3.2. ARTs in yeast and fungi; 3.3. Amoebal ADCs.
- 4. Other Arrestin-Fold Proteins4.1. VPS26, a component of the retromer; 4.1.1. Crystal structure of retromer subunits; 4.1.2. Regulation of the retromer�s function; 4.2. DSCR3, a VPS26-related protein; 4.3. RGP1, yet another arrestin-fold protein; 5. Are Arrestins and Arrestin-Fold Proteins Related by a Shared Mechanism for Their Function?; 6. Conclusion and Perspectives; References; Chapter Three: Structural Determinants of Arrestin Functions; 1. Introduction; 2. What the Crystal Structure Reveals, and What It Does Not; 3. How Do Arrestins Fit Receptors?
- 3.1. Receptor-binding surface of arrestins3.2. The stoichiometry of the complex; 3.3. Phosphate-binding residues and the phosphate sensor; 3.4. The conformation of the receptor-bound arrestin; 3.5. Key determinants of receptor preference; 4. Interactions with Other Signaling Proteins; 4.1. Where do the other partners bind?; 4.2. The shape of the arrestin-MAPK signaling complex; 4.3. Conformational preferences determine outcomes; 4.4. Binding and activation do not go hand-in-hand; 5. Designing Signaling-Biased Arrestin Mutants; 5.1. Enhanced phosphorylation-independent mutants.
- 5.2. Constitutively monomeric arrestins5.3. Manipulating MAPK signaling; 6. Conclusions: Where Do We Go from Here?; Acknowledgments; References; Chapter Four: Arrestins: Role in the Desensitization, Sequestration, and Vesicular Trafficking of G Protein-Coupled Receptors; 1. Introduction; 2. Arrestins in GPCR Desensitization; 3. Arrestins in GPCR Trafficking; 3.1. Sequestration; 3.2. Postendocytic vesicular trafficking of GPCRs; 4. Conclusions; Acknowledgments; References; Chapter Five: Arrestins as Regulators of Kinases and Phosphatases; 1. Introduction; 2. Arrestins as GPCR Effectors.