The Ubiquitin System in Health and Disease
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Ernst Schering Foundation Symposium Proceedings 2008-1
The Ubiquitin System in Health and Disease S. Jentsch, B. Haendler Editors With 39 Figures
123
Series Editors: G. Stock and C. Klein
Library of Congress Control Number: 2008935386 ISSN 0947-6075 ISBN 978-3-540-85106-6 Springer Berlin Heidelberg New York This work is subject to copyright. All rights are reserved, 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 way, and storage in data banks. Duplication of this publication or parts thereof is permitted only under the provisions of the German Copyright Law of September 9, 1965, in its current version, and permission for use must always be obtained from Springer-Verlag. Violations are liable for prosecution under the German Copyright Law. Springer is a part of Springer Science+Business Media springer.com © Springer-Verlag Berlin Heidelberg 2009 The use of general descriptive names, registered names, trademarks, etc. in this publication does not emply, even in the absence of a specific statemant, that such names are exempt from the relevant protective laws and regulations and therefor free for general use. Product liability: The publisher cannot guarantee the accuracy any information about dosage and application contained in this book. In every induvidual case the user must check such information by consulting the relevant literature. Cover design: WMXDesign, Heidelberg Typesetting and production: le-tex publishing services oHG, Leipzig 21/3180/YL – 5 4 3 2 1 0 Printed on acid-free paper
Preface
The ubiquitin system has two major functions in eukaryotic cells: it regulates protein degradation, which is essential for normal cellular function and for the removal of potentially harmful, damaged, or misfolded proteins, and it controls protein activity by regulating protein–protein interactions and subcellullar localization. The ubiquitin system is thus involved in processes as diverse as cell cycle progression, signal transduction, gene transcription, and DNA repair. Not surprisingly, defects in the ubiquitin system have been linked with numerous diseases such as cancer, inflammation, central nervous system disorders, and metabolic dysfunction. Ubiquitin is a highly conserved 76-amino acid protein which is transferred to its target protein in an ATP-dependent manner. This post-translational modification takes place in a hierarchical, three-step fashion involving an E1 ubiquitin-activating enzyme, an E2 ubiquitinconjugating enzyme, and an E3 ubiquitin ligase. Substrate specificity is predominantly controlled by members of a large family of E3 enzymes, which form complexes with the proteins that will be modified. This ultimately leads to the covalent attachment of the C-terminus of ubiquitin to usually an ε-amino group of a lysine residue in the targeted protein. Additional ubiquitin transfer to lysine-48 of ubiquitin itself will form a polyubiquitin chain, whic
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