Arrestins

Arrestins

Structure and Function in Vision and Beyond

1st Edition - March 20, 2022

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  • Editor: Vsevolod Gurevich
  • Paperback ISBN: 9780323857567
  • eBook ISBN: 9780323856355

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Description

Arrestins: Structure and Function in Vision and Beyond examines the structural basis of the function of arrestin proteins in the brain. Linking basic, translational and clinical research, this volume begins with history and basic signaling principles and then expands to the use of proteins as potential therapeutic targets. Multiple cellular activities are detailed, including activation, signaling, GPCR endocytosis, and ERK signaling, with chapters examining both visual and non-visual arrestins. Experts in their respective fields are featured throughout, making this book essential reading for anyone who wants to explore the basic science underlying these signaling proteins.

Key Features

  • Links basic, translational and clinical research on arrestin and GPCR signaling proteins in the nervous system
  • Features chapters on arrestins' vital signaling functions in brain health
  • Includes unique sections on their use as potential therapeutic targets
  • Covers both vision and non-vision arrestins
  • Provides an overview for scientists new to the study of GPCRs and arrestins

Readership

Cellular/molecular neuroscientists at the graduate/postgraduate level

Table of Contents

  • Cover image
  • Title page
  • Table of Contents
  • Copyright
  • Contributors
  • Preface
  • Chapter 1. History of arrestins
  • Chapter 2. Arrestin-mediated trafficking and compartmentalized biology of GPCRs
  • 1. Introduction
  • 2. Arrestin as a scaffold for endocytic proteins
  • 3. Molecular determinates guiding receptor trafficking: Class A versus Class B GPCRs
  • 4. Arrestin as a spatiotemporal regulator of G protein signaling
  • 5. Arrestin-dependent ubiquitination and postendocytic sorting
  • 6. Conclusion
  • Chapter 3. The structural basis of arrestin–GPCR interactions
  • 1. GPCRs go through an activation–inactivation cycle
  • 2. Inactive arrestins adopt an autoinhibitory conformation
  • 3. Binding of a phosphorylated GPCR C-tail peptide is sufficient to activate arrestin
  • 4. The active state arrestin crest loops bind the cytoplasmic surface of active state GPCRs
  • 5. Advancements in cryo-EM have enabled the recent determination of additional GPCR-G protein and GPCR–arrestin structures
  • 6. Finger loop variability and dynamics contribute to β-arrestin's GPCR-binding promiscuity
  • 7. Signaling selectivity: phosphorylation bar codes and structural determinants of biased signaling
  • Chapter 4. Arrestin scaffolding and activation of MAPK cascades
  • 1. Introduction
  • 2. Arrestin and the Raf-MEK-ERK cascade
  • 3. Arrestin and the ASK1-MKK4/7-JNK3 cascade
  • 4. Arrestin and the ASK1-MKK3/6-p38 cascade
  • 5. Concluding Remarks
  • Chapter 5. β-Arrestins as regulators of key metabolic processes
  • 1. Introduction
  • 2. Canonical functions of βarr2 in disrupting signaling through metabolically important GPCRs
  • 3. Noncanonical functions of β-arrestins: modulation of the activity of cytoplasmic signaling proteins
  • 4. Noncanonical functions of β-arrestins: role of nuclear βarr1 in regulating metabolic processes
  • 5. Concluding remarks
  • Chapter 6. Arrestins in cardiac function: the current state of affairs
  • 1. Introduction
  • 2. Cardiac adrenergic receptors and βarrestins
  • 3. Cardiac angiotensin II receptors and βarrestins
  • 4. Other cardiac GPCRs and βarrestins
  • 5. Conclusions and future perspectives
  • Chapter 7. Signaling-biased arrestin-based molecular tools
  • 1. Introduction
  • 2. Structure of arrestins: functional role of select elements
  • 3. Altered receptor specificity of arrestins can bias signaling
  • 4. Manipulation of GPCR trafficking by arrestin mutants can also bias signaling
  • 5. Biasing signaling by altering effector binding
  • 6. Limitations for construction of designer arrestins: cross-talk in the arrestin molecule
  • 7. Barcode hypothesis and its implications for biased signaling
  • 8. What needs to be done next to create signaling-biased arrestin-based tools?
  • Index

Product details

  • No. of pages: 142
  • Language: English
  • Copyright: © Academic Press 2022
  • Published: March 20, 2022
  • Imprint: Academic Press
  • Paperback ISBN: 9780323857567
  • eBook ISBN: 9780323856355

About the Editor

Vsevolod Gurevich

Dr. Gurevich obtained his PhD at the Shemyakin Institute of Bioorganic Chemistry, in Moscow, Russia. He performed his postdoctoral studies at Thomas Jefferson University in Philadelphia and is currently Professor of Pharmacology at Vanderbilt University. He is a Cornelius Vanderbilt Endowed Chair. He has published more than 220 papers in reputed journals and has been serving as an editorial board member of several journals. The main focus of the work in his lab is structure-function studies of arrestins, that bind almost all of >800 G protein-coupled receptors in humans and dozens of non-receptor signaling proteins. The lab is using biochemistry, biophysics, and cell biology to elucidate arrestin elements involved in the interactions with various binding partners and to construct signaling-biased arrestins specifically targeting individual receptors and signaling pathways.

Affiliations and Expertise

Professor of Pharmacology, Vanderbilt University Medical Center, USA

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