Protein Secretion Methods and Protocols
Over the past thirty years, many elegant genetic and biochemical approaches have been combined in order to advance the study of protein secretion and the necessary navigation through cell membranes, yet, despite this progress, less than two hundred membra
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MO L E C U L A R BI O L O G Y
Series Editor John M. Walker School of Life Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For other titles published in this series, go to www.springer.com/series/7651
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Protein Secretion Methods and Protocols
Edited by
Anastassios Economou Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology - Hellas, Heraklion, Greece
Editor Anastassios Economou Foundation for Research & Technology − Hellas (FORTH) Institute of Molecular Biology & Biotechnology and Department of Biology University of Crete Nikolaou Plastira 100 700 13 Iraklion Greece [email protected]
ISSN 1064-3745 e-ISSN 1940-6029 ISBN 978-1-60327-167-7 e-ISBN 978-1-60327-412-8 DOI 10.1007/978-1-60327-412-8 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2010920086 © Springer Science+Business Media, LLC 2010 All rights reserved. This work may not be translated or copied in whole or in part without the written permission of the publisher (Humana Press, c/o Springer Science+Business Media, LLC, 233 Spring Street, New York, NY 10013, USA), except for brief excerpts in connection with reviews or scholarly analysis. Use in connection with any form of information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed is forbidden. The use in this publication of trade names, trademarks, service marks, and similar terms, even if they are not identified as such, is not to be taken as an expression of opinion as to whether or not they are subject to proprietary rights. Printed on acid-free paper Humana Press is part of Springer Science+Business Media (www.springer.com)
Preface The elucidation of the complete information content in hundreds of genomes has brought with it a surprising realization. More than a third of all the proteins in any given proteome are comprised of non-cytoplasmic polypeptides. These can be resident membrane proteins such as channels and receptors or secretory proteins such as hydrolytic enzymes and toxins. Membrane biogenesis and protein trafficking and secretion are central to the biology and pathology of the cell. Optimal protein trafficking is essential for cell viability, communication, and programmed death, for cells to modulate and yield metabolic goods from their environment, for pathogens to attack, and for hosts to fend them off. Since all polypeptides in prokaryotes and most in eukaryotes are synthesized by cytoplasmic ribosomes, the cell has acquired tools that enable it to accurately and efficiently sort exported proteins from the cytoplasmic residents. Various specialized chaperones, pilots, and ushers have evolved to correctly recognize secretory and membrane proteins and in several instances this recognition prevents or stalls folding reactions. Moreover, this chaperone-mediated “face-control” effectively sorts extra-cytoplasmic from cytoplasmic proteins and then delivers them to complex membrane-associ
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