Protein Lipidation Methods and Protocols
This volume explores techniques used to detect lipids attached to proteins, to analyze the function of lipid modifications, and to characterize the enzymes that add and remove lipids from proteins. The book is organized into seven parts: Part One describe
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Maurine E. Linder Editor
Protein Lipidation Methods and Protocols
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
Protein Lipidation Methods and Protocols
Edited by
Maurine E. Linder Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA
Editor Maurine E. Linder Department of Molecular Medicine College of Veterinary Medicine Cornell University Ithaca, NY, USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-9531-8 ISBN 978-1-4939-9532-5 (eBook) https://doi.org/10.1007/978-1-4939-9532-5 © Springer Science+Business Media, LLC, part of Springer Nature 2019 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. This Humana imprint is published by the registered company Springer Science+Business Media, LLC part of Springer Nature. The registered company address is: 233 Spring Street, New York, NY 10013, U.S.A.
Preface Posttranslational modifications of proteins diversify the proteome and can be regulated or regulatory. In eukaryotic cells, protein lipidation encompasses a variety of lipid modifications that contribute to protein localization and function, with fatty acylation and isoprenylation among the most abundant. Fatty acids are attached to proteins through thioester linkage at cysteine (S-acylation, typically S-palmitoylation), amide linkage at lysine or an aminoterminal glycine or cysteine (N-acylation), and oxyester linkage to serine (O-acylation). A stable modification for some proteins, fatty acylation is reversible for others. Isoprenylation of proteins occurs at C-terminal cysteine motifs in which a C15-farnesyl or C20-geranylgeranyl isoprenoid is added through a stable thioether linkage. Pro
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