The Structural Basis of Arrestin Functions

This volume summarizes our current understanding of the structural basis of the functions of arrestin family of proteins. Arrestins were first discovered as key players in the desensitization of G protein-coupled receptors (GPCRs). Recent studies showed t

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The Structural Basis of Arrestin Functions

The Structural Basis of Arrestin Functions

Vsevolod V. Gurevich Editor

The Structural Basis of Arrestin Functions

123

Editor Vsevolod V. Gurevich Department of Pharmacology Vanderbilt University Nashville, TN USA

ISBN 978-3-319-57552-0 DOI 10.1007/978-3-319-57553-7

ISBN 978-3-319-57553-7

(eBook)

Library of Congress Control Number: 2017938139 © Springer International Publishing AG 2017 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. Printed on acid-free paper This Springer imprint is published by Springer Nature The registered company is Springer International Publishing AG The registered company address is: Gewerbestrasse 11, 6330 Cham, Switzerland

Preface

Arrestin, like all key players in the G protein-coupled receptor (GPCR) signaling, was first discovered in the visual system, where it was shown to specifically bind active phosphorylated rhodopsin, “arresting” its coupling to a cognate G protein. Subsequently, three homologues of visual arrestin were cloned and functionally characterized. All members of the arrestin family bind active phosphorylated forms of their cognate receptors and stop G protein-mediated signaling of most GPCRs. Structurally *45 kDa arrestin proteins are elongated two-domain molecules with the overall fold shared with (likely inherited from) arrestin domain-containing proteins (ARRDCs) involved in trafficking of membrane vesicles and proteins. Vertebrates (except bony fish that underwent an additional whole-genome duplication event) express only four arrestin subtypes, whereas other animals have even fewer arrestins. Recently, the focus has shifted to the non-visual arrestins, two subtypes of which are expressed in every vertebrate species. These two arrestins bind hundreds of different GPCRs and interact with numerous non-receptor partners, including various trafficking and signaling prot