SUMO Regulation of Cellular Processes PDF
Preview SUMO Regulation of Cellular Processes
Advances in Experimental Medicine and Biology 963 Van G. Wilson Editor SUMO Regulation of Cellular Processes Second Edition Advances in Experimental Medicine and Biology Volume 963 Editorial Board IRUN R. COHEN, The Weizmann Institute of Science, Rehovot, Israel ABEL LAJTHA, N.S. Kline Institute for Psychiatric Research, Orangeburg, NY, USA JOHN D. LAMBRIS, University of Pennsylvania, Philadelphia, PA, USA RODOLFO PAOLETTI, University of Milan, Milan, Italy Advances in Experimental Medicine and Biology presents multidisciplinary and dynamic findings in the broad fields of experimental medicine and biology. The wide variety in topics it presents offers readers multiple perspectives on a variety of disciplines including neuroscience, microbiology, immunology, biochemistry, biomedical engineering and cancer research. Advances in Experimental Medicine and Biology has been publishing exceptional works in the field for over 30 years and is indexed in Medline, Scopus, EMBASE, BIOSIS, Biological Abstracts, CSA, Biological Sciences and Living Resources (ASFA-1), and Biological Sciences. The series also provides scientists with up to date information on emerging topics and techniques. More information about this series at http://www.springer.com/series/5584 Van G. Wilson Editor SUMO Regulation of Cellular Processes Second Edition Editor Van G. Wilson Department of Microbial Pathogenesis and Immunology, College of Medicine Texas A&M Health Science Center Bryan, TX, USA ISSN 0065-2598 ISSN 2214-8019 (electronic) Advances in Experimental Medicine and Biology ISBN 978-3-319-50043-0 ISBN 978-3-319-50044-7 (eBook) DOI 10.1007/978-3-319-50044-7 Library of Congress Control Number: 2017932104 1st edition: © Springer Science+Business Media B.V. 2009 © Springer International Publishing AG 2017 Chapter 11 was created within the capacity of an US governmental employment. US copyright protection does not apply. 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. Printed on acid-free paper This Springer imprint is published by Springer Nature The registered company is Springer International Publishing AG The registered company address is: Gewerbestrasse 11, 6330 Cham, Switzerland Preface Posttranslational modification of proteins has proven to be a critical regula- tory mechanism to control protein function, location, and interaction with partners. In 1996 several groups independently identified a new protein modi- fier moiety that has become known as SUMO (small ubiquitin-like modifier). It was quickly established that SUMO is part of a larger ubiquitin superfamily and that the enzymology of SUMO addition to substrates paralleled the canonical ubiquitin modification pathway. Early studies in the field of sumoylation examined single protein substrates, and the total number of known substrates grew slowly for the first 15 years after the discovery of SUMO. Much of this early work focused on transcription factors as they were among the first identified substrates for sumoylation. A large literature estab- lished a critical regulatory role for sumoylation in fine-tuning many transcrip- tional units that impacted a variety of cellular systems including development and differentiation; cell growth and division; DNA organization, replication, and repair; and defense from pathogens. As would be expected given the involvement of sumoylation in so many fundamental cellular processes, mutations affecting the sumoylation components typically result in lethal or severely dysfunctional phenotypes. Additionally, disruption of SUMO homeostasis was shown to contribute to the development and establishment of some oncogenic malignancies. In the years since the original edition of this book, there has been an enor- mous increase in the interest in and understanding of the widespread role of sumoylation in biological processes. The application of proteomics approaches in the mid-2000s rapidly expanded the identification of SUMO substrates along with the mapping of sumoylation sites in these substrates. This enlarged cohort of substrates revealed new pathways and processes modulated by sumoylation and confirmed that sumoylation is a globally sig- nificant regulator of cellular biology. It also became clear that the original definition of a SUMO accepter site accounted for only a portion of the mapped sites, leading to the elucidation of several other types of consensus acceptor motifs. Other advances include an increasing appreciation of the role of sumoylation in network coordination (mediated via SUMO-modified proteins binding to proteins with specific SUMO-interacting motifs), of the importance of cross talk between the SUMO and ubiquitin systems, and of the critical contributions of sumoylation to host health and defense against v vi Preface pathogens. All of these topics are addressed in revised or new chapters of this edition, and the contributors hope that this book will provide both a strong foundation of established information in this field and an introduction to cutting- edge finding and unanswered questions. Bryan, TX, USA Van G. Wilson Contents 1 Introduction to Sumoylation ....................................................... 1 Van G. Wilson Part I Molecular Functions 2 Roles of Sumoylation in mRNA Processing and Metabolism ............................................................................ 15 Patricia Richard, Vasupradha Vethantham, and James L. Manley 3 SUMO and Chromatin Remodeling ........................................... 35 David Wotton, Lucy F. Pemberton, and Jacqueline Merrill-Schools 4 Functions of SUMO in the Maintenance of Genome Stability ...................................................................... 51 Nicola Zilio, Karolin Eifler-Olivi, and Helle D. Ulrich 5 Regulation of Cellular Processes by SUMO: Understudied Topics .................................................................... 89 Jorrit M. Enserink 6 The Molecular Interface Between the SUMO and Ubiquitin Systems ................................................................. 99 Jeff L. Staudinger 7 SUMO and Nucleocytoplasmic Transport ................................. 111 Christopher Ptak and Richard W. Wozniak 8 Sumo Modification of Ion Channels ........................................... 127 Mark Benson, Jorge A. Iñiguez-lluhí, and Jeffrey Martens 9 The Roles of SUMO in Metabolic Regulation ........................... 143 Elena Kamynina and Patrick J. Stover Part II Cell Growth Regulation 10 The SUMO Pathway in Mitosis .................................................. 171 Debaditya Mukhopadhyay and Mary Dasso vii viii Contents 11 Wrestling with Chromosomes: The Roles of SUMO During Meiosis ............................................................ 185 Amanda C. Nottke, Hyun-Min Kim, and Monica P. Colaiácovo 12 Sumoylation in Development and Differentiation ..................... 197 Adeline F. Deyrieux and Van G. Wilson 13 The Role of Sumoylation in Senescence ..................................... 215 Lyndee L. Scurr, Sebastian Haferkamp, and Helen Rizos 14 Regulation of Plant Cellular and Organismal Development by SUMO ............................................................... 227 Nabil Elrouby 15 SUMO in Drosophila Development ............................................ 249 Joseph Cao and Albert J. Courey Part III Diseases 16 Sumoylation: Implications for Neurodegenerative Diseases ......................................................................................... 261 Dina B. Anderson, Camila A. Zanella, Jeremy M. Henley, and Helena Cimarosti 17 Sumoylation and Its Contribution to Cancer ............................ 283 Jason S. Lee, Hee June Choi, and Sung Hee Baek 18 Sumoylation Modulates the Susceptibility to Type 1 Diabetes ........................................................................ 299 Jing Zhang, Zhishui Chen, Zhiguang Zhou, Ping Yang, and Cong-Yi Wang 19 Sumoylation in Craniofacial Disorders ...................................... 323 Erwin Pauws and Philip Stanier 20 Coordination of Cellular Localization-Dependent Effects of Sumoylation in Regulating Cardiovascular and Neurological Diseases ........................................................... 337 Jun-ichi Abe, Uday G. Sandhu, Nguyet Minh Hoang, Manoj Thangam, Raymundo A. Quintana-Quezada, Keigi Fujiwara, and Nhat Tu Le 21 Viral Interplay with the Host Sumoylation System .................. 359 Van G. Wilson 22 Sumoylation as an Integral Mechanism in Bacterial Infection and Disease Progression .............................................. 389 Chittur V. Srikanth and Smriti Verma Index ...................................................................................................... 409 1 Introduction to Sumoylation Van G. Wilson Abstract Reversible post-translational modification is a rapid and efficient system to control the activity of pre-existing proteins. Modifiers range from small chemical moieties, such as phosphate groups, to proteins themselves as the modifier. The patriarch of the protein modifiers is ubiquitin which plays a central role in protein degradation and protein targeting. Over the last 20 years, the ubiquitin family has expanded to include a variety of ubiquitin-related small modifier proteins that are all covalently attached to a lysine residue on target proteins via series of enzymatic reactions. Of these more recently discovered ubiquitin-like proteins, the SUMO family has gained prominence as a major regulatory component that impacts numerous aspects of cell growth, differentiation, and response to stress. Unlike ubiquitinylation which often leads to proteins turn over, sumoylation performs a variety of function such as altering protein stability, modulat- ing protein trafficking, directing protein-protein interactions, and regulat- ing protein activity. This chapter will introduce the basic properties of SUMO proteins and the general tenets of sumoylation. Keywords SUMO • Ubc9 • SAE1/2 • SENP • SUMO Ligases 1.1 The Sumo Proteins Over two decades ago, a small cellular protein of 12 kDa, with 18% homology to the well-known V.G. Wilson (*) ubiquitin protein, was co-discovered and termed Department of Microbial Pathogenesis and Small Ubiquitin-like MOdifier or SUMO. SUMO Immunology, College of Medicine, Texas A&M was independently identified by four groups in Health Science Center, 8447 HWY 47, Bryan, 1996: Freemont’s group found it as a small TX 77807-1359, USA e-mail: [email protected] ubiquitin-l ike protein associated with PML in an © Springer International Publishing AG 2017 1 V.G. Wilson (ed.), SUMO Regulation of Cellular Processes, Advances in Experimental Medicine and Biology 963, DOI 10.1007/978-3-319-50044-7_1
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