Hedgehog Signaling Protocols
The second edition of this volume provides novel protocols for the study of newly discovered function and modifications of components of the Hh pathways. The first few chapters discuss methods for stable delivery of soluble Hh proteins in cell cultures th
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Natalia A. Riobo Editor
Hedgehog Signaling Protocols Second Edition
METHODS
IN
MOLECULAR BIOLOGY
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Hedgehog Signaling Protocols Second Edition
Edited by
Natalia A. Riobo Department of Biochemistry and Molecular Biology, Sidney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA
Editor Natalia A. Riobo Department of Biochemistry and Molecular Biology Sidney Kimmel Cancer Center Thomas Jefferson University Philadelphia, PA, USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-2771-5 ISBN 978-1-4939-2772-2 (eBook) DOI 10.1007/978-1-4939-2772-2 Library of Congress Control Number: 2015942639 Springer New York Heidelberg Dordrecht London © Springer Science+Business Media New York 2015 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. Printed on acid-free paper Humana Press is a brand of Springer Springer Science+Business Media LLC New York is part of Springer Science+Business Media (www.springer.com)
Preface Posttranslational Modifications and Secretion of the Hedgehog (Hh) Proteins Mammalian genomes contain three homologs of the Drosophila Hh protein—Sonic (Shh), Indian (Ihh), and Desert (Dhh), encoded by separate genes [1]. All Hh proteins are autoprocessed and posttranslationally modified in a similar manner before being secreted by the producing cell and received by surrounding tissues. Coincidentally, Hh proteins share a high homology in their C-terminal half, similar to the intein regions of self-splicing proteins of bacteria that undergo intramolecular processing. Autoprocessing occurs in the endoplasmic reticulum where the signal sequence of the Hh precursor is first cleaved. The C-terminal autoprocessing domain of Hh catalyzes the self-cleavage by an internal Cys nucleophilic attack on a peptide bond, which is resolv
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