Reviews of Physiology, Biochemistry and Pharmacology
H. Wegele, L. Müller, and J. Buchner: Hsp70 and Hsp90 – A Relay Team for Protein Folding R. Schülein: The Early Stages of the Intracellular Transport of Membrane Proteins: Clinical and Pharmacological Implications L. Schild: The Epithelial Sodium Channel:
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151 Physiology Biochemistryand Pharmacology Editors S.G. Amara, Portland • E. Bamberg, Frankfurt H. Grunicke, Innsbruck • R. Jahn, G6ttingen W.J. Lederer, Baltimore • A. Miyajima, Tokyo H. Murer, Ztirich • S. Offermanns, Heidelberg G. Schultz, Berlin • M. Schweiger, Berlin
With 15 Figures
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ISSN 0303-4240 ISBN 3-540-22096-8 Springer-Verlag Berlin Heidelberg New York Library of Congress-Catalog-Card Number 74-3674 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 SpringerVerlag. Violations are liable for prosecution under the German Copyright Law. Springer-Verlag is a part of Springer Science+Business Media springeronline.com © Springer-Verlag Berlin Heidelberg 2004 Printed in Germany The use of general descriptive names, registered names, trademarks, 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. Product liability: The publishers cannot guarantee the accuracy of any information about dosage and application contained in this book. In every individual case the user must check such information by consulting the relevant literature. Editor: Dr. Thomas Mager, Heidelberg Desk editor: Anne Clauss, Heidelberg Production editor: Dagmar Orth, Andreas GOsling, Heidelberg Cover design: design & production GmbH, Heidelberg Typesetting: Sttirtz AG, WUrzburg Printed on acid-free p a p e r - 14/3150 ag
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Rev Physiol Biochem Pharmacol (2004) 151:1–44 DOI 10.1007/s10254-003-0021-1
H. Wegele · L. Mller · J. Buchner
Hsp70 and Hsp90—a relay team for protein folding
Published online: 23 January 2004 Springer-Verlag 2004
Abstract Molecular chaperones are a functionally defined set of proteins which assist the structure formation of proteins in vivo. Without certain protective mechanisms, such as binding nascent polypeptide chains by molecular chaperones, cellular protein concentrations would lead to misfolding and aggregation. In the mammalian system, the molecular chaperones Hsp70 and Hsp90 are involved in the folding and maturation of key regulatory proteins, like steroid hormone receptors, transcription factors, and kinases, some of which are involved in cancer progression. Hsp70 and Hsp90 form a multichaperone complex, in which both are connected by a third protein called Hop. The connection of and the interplay between the two chaperone machineries is of crucial importance for cell viability. This review provides a detailed view of the Hsp70 and Hsp90 machineries, their cofactors and their mode
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