Wilson / Willson SUMO Regulation of Cellular Processes
2009
ISBN: 978-90-481-2649-1
Verlag: Springer Netherland
Format: EPUB
Kopierschutz: 6 - ePub Watermark
E-Book, Englisch, 339 Seiten, eBook
ISBN: 978-90-481-2649-1
Verlag: Springer Netherland
Format: EPUB
Kopierschutz: 6 - ePub Watermark
Zielgruppe
Research
Autoren/Hrsg.
Weitere Infos & Material
1;Contents;4
2;Contributors;6
3;1 Introduction to Sumoylation;9
3.1;1.1 The SUMO Proteins;9
3.2;1.2 The Enzymology of Sumoylation;11
3.3;1.3 Sumoylation Functions;13
3.4;1.4 Conclusion;14
3.5;References;15
4;Part I Molecular Functions;19
4.1;2 SUMO Modification and Transcriptional Regulation;20
4.1.1;2.1 Introduction;20
4.1.2;2.2 Sumoylation of Sequence Specific Regulators;24
4.1.2.1;2.2.1 Direct Effects on DNA Binding: HSF2;24
4.1.2.2;2.2.2 Sumoylation of Precursors and Regulatory Subunits: NF B ;25
4.1.2.3;2.2.3 Sumo as a Modulator of Transcriptional Regulatory Potential;25
4.1.2.3.1;2.2.3.1 Effect on Activators;26
4.1.2.3.2;2.2.3.2 Basis for the Promoter Context Dependence of Sumoylation;27
4.1.2.3.3;2.2.3.3 Sumoylation of Repressors: Positive Effects;28
4.1.2.3.4;2.2.3.4 Sumoylation of Repressors: Negative Effects;30
4.1.3;2.3 SUMO Harbors an Intrinsic Transcriptional Inhibitory Function;31
4.1.3.1;2.3.1 Identification of an Effector Surface in SUMO That Interacts with Sumo Binding Motifs;32
4.1.3.2;2.3.2 What Are the Mediators of the Repressive Effects of SUMO?;33
4.1.4;2.4 Sumoylation of Coregulators;35
4.1.4.1;2.4.1 Coactivators;36
4.1.4.2;2.4.2 Corepressors;38
4.1.5;2.5 How Does SUMO Modification Exerts Significant Effects at Low Stoichiometries?;40
4.1.6;2.6 Coda;42
4.1.7;References;43
4.2;3 Emerging Roles for SUMO in mRNA Processing and Metabolism;48
4.2.1;3.1 A Brief Introduction to RNA Processing Events, Interconnections to Transcription and Export;48
4.2.2;3.2 RNA Processing Factors as Sumoylation Substrates;49
4.2.3;3.3 5 Capping;50
4.2.4;3.4 Splicing;53
4.2.5;3.5 3 End Processing;54
4.2.6;3.6 Sumoylation of hnRNPS;57
4.2.7;3.7 Extending the Role of SUMO to mRNA Export;58
4.2.8;3.8 SUMO and RNA Editing;59
4.2.9;3.9 Conclusions;59
4.2.10;References;60
4.3;4 SUMO and Chromatin Remodelling;65
4.3.1;4.1 Introduction;66
4.3.2;4.2 Histone Sumoylation;66
4.3.3;4.3 SUMO and Higher Order Chromatin Structure;68
4.3.4;4.4 Telomeres and Centromeres;70
4.3.5;4.5 SUMO-Dependent Recruitment of General Transcriptional Corepressors;72
4.3.5.1;4.5.1 SUMO-Dependent HDAC Recruitment;72
4.3.5.2;4.5.2 Corepressor Complex Recruitment;73
4.3.6;4.6 SUMO-Dependent Modulation of General Coregulator Activity;74
4.3.6.1;4.6.1 HDAC Sumoylation and HDAC-Dependent Sumoylation;74
4.3.6.2;4.6.2 Sumoylation of General Transcriptional Corepressors;75
4.3.7;4.7 The Role of SUMO E3 Ligases in Chromatin Remodelling;76
4.3.8;References;78
4.4;5 Functions of SUMO in the Maintenance of Genome Stability;83
4.4.1;5.1 Introduction;84
4.4.2;5.2 Effects of SUMO on Homologous Recombination;85
4.4.2.1;5.2.1 Mms21-Dependent Sumoylation;86
4.4.2.2;5.2.2 Sumoylation of Rad52;86
4.4.2.3;5.2.3 Sumoylation of PCNA;88
4.4.3;5.3 Sumoylation of Thymidine DNA Glycosylase in Base Excision Repair;89
4.4.4;5.4 Function of SUMO in the Maintenance of Telomere Length;90
4.4.5;5.5 Sumoylation of Topoisomerase II in Chromosome Segregation;92
4.4.6;5.6 Function of Poly-SUMO Chains in DNA Repair;94
4.4.7;5.7 Conclusion;96
4.4.8;References;97
4.5;6 SUMO and Nucleocytoplasmic Transport;103
4.5.1;6.1 Introduction;103
4.5.2;6.2 Compartment-Specific Sumoylation;106
4.5.3;6.3 Regulation of Nuclear Transport by Sumoylation;108
4.5.3.1;6.3.1 SUMO-Dependent Inhibition of Nuclear Export;109
4.5.3.2;6.3.2 SUMO-dependent Stimulation of Nuclear Export;112
4.5.3.3;6.3.3 Sumoylation and Nuclear Import;112
4.5.4;6.4 Control of the Nuclear Transport Machinery by Sumoylation;114
4.5.5;6.5 Nucleocytoplasmic Transport of SUMO-Specific Enzymes;115
4.5.6;6.6 Conclusion;116
4.5.7;References;117
4.6;7 SUMO Modification of Ion Channels;123
4.6.1;7.1 Introduction;123
4.6.2;7.2 Extranuclear Targets of Sumoylation;125
4.6.3;7.3 Sumoylation of Ion Channels;127
4.6.3.1;7.3.1 K2P1;127
4.6.3.2;7.3.2 Kv1.5;131
4.6.3.3;7.3.3 GluR6;133
4.6.4;7.4 Ion Channels as Probes of SUMO Modification at the Plasma Membrane;135
4.6.5;7.5 Conclusions;139
4.6.6;References;140
4.7;8 The Roles of SUMO in Metabolic Regulation;143
4.7.1;8.1 Introduction: Functions of SUMO in Metabolism;144
4.7.2;8.2 SUMO and Master Regulation of Lipid Biosynthesis;144
4.7.3;8.3 Metabolic Adaptation to Cellular and Oxidative Stress;146
4.7.4;8.4 SUMO and Energy Metabolism;147
4.7.4.1;8.4.1 SUMO and Muscle Metabolism;147
4.7.4.2;8.4.2 SUMO and Insulin Synthesis;148
4.7.4.3;8.4.3 SUMO and Glucose Transport;149
4.7.4.4;8.4.4 Mitochondrial Biogenesis and Metabolic Disease;150
4.7.5;8.5 SUMO and Folate-Mediated One-Carbon Metabolism;151
4.7.6;References;153
5;Part II Cell Growth Regulation;156
5.1;9 The SUMO Pathway in Mitosis;157
5.1.1;9.1 Introduction;157
5.1.2;9.2 The SUMO Pathway;158
5.1.3;9.3 Outcomes of SUMO Modification;159
5.1.4;9.4 The Role of SUMO in Mitotic Chromosome Structure;160
5.1.5;9.5 SUMO and Centromere/Kinetochore Organization;163
5.1.6;9.6 SUMO and Cytokinesis;167
5.1.7;9.7 Conclusions and Perspectives;168
5.1.8;References;169
5.2;10 Wrestling with Chromosomes: The Roles of SUMODuring Meiosis;174
5.2.1;10.1 Introduction;174
5.2.2;10.2 Sumoylation;175
5.2.2.1;10.2.1 Sumoylation in Meiosis: A Phenotypic Survey;177
5.2.2.2;10.2.2 Targets of Sumoylation in Meiosis;179
5.2.3;10.3 Centromeric Heterochromatin and Sumoylation;179
5.2.4;10.4 Centromeric Coupling;180
5.2.5;10.5 SUMO-Mediated Regulation of SC Dynamics;182
5.2.5.1;10.5.1 ZIP1 and ZIP3: A SUMO Connection;182
5.2.6;10.6 Meiotic DSB Repair/Recombination;184
5.2.7;10.7 Conclusions;185
5.2.8;References;186
5.3;11 Sumoylation in Development and Differentiation;189
5.3.1;11.1 Introduction;189
5.3.2;11.2 The Reproductive System;190
5.3.2.1;11.2.1 Gonadal, Uterine, and Vuval Morphogenesis;190
5.3.2.2;11.2.2 Sperm Differentiation;191
5.3.3;11.3 Stem Cell Differentiation;193
5.3.3.1;11.3.1 Embryonic Stem Cells Diffentiation;193
5.3.3.2;11.3.2 Hematopoietic Stem Cells -- Macrophage Differentiation;194
5.3.4;11.4 Tissue and Cellular Differentiation;195
5.3.4.1;11.4.1 Keratinocytes;195
5.3.4.2;11.4.2 Myocytes;196
5.3.4.3;11.4.3 Neuronal Cells;197
5.3.5;11.5 Conclusions;198
5.3.6;References;199
5.4;12 The Role of Sumoylation in Senescence;202
5.4.1;12.1 Introduction;202
5.4.2;12.2 Sumoylation and Senescence;205
5.4.3;12.3 Cellular Senescence and p53 Sumoylation;207
5.4.4;12.4 Sumoylation, Senescence, and the Retinoblastoma Protein;208
5.4.5;12.5 Role of PML and Sumoylation in the Regulation of Senescence;210
5.4.6;12.6 Telomere Maintenance and SUMO;211
5.4.7;12.7 Conclusions;212
5.4.8;References;213
5.5;13 Sumoylation and Apoptosis;218
5.5.1;13.1 Introduction;218
5.5.2;13.2 p53 as a Major Apoptosis Regulatory Gene;219
5.5.2.1;13.2.1 P53 and Hematological Malignancies;220
5.5.2.2;13.2.2 Nutlin-3 Dependent Apoptosis;221
5.5.3;13.3 Aging and Apoptosis;223
5.5.4;13.4 Hormone Nuclear Receptor and Acetylation/Sumoylation;224
5.5.5;13.5 Sumoylation and Mitochondria-Associated Apoptosis;225
5.5.6;13.6 Topoisomerase as a Target of Apoptosis;226
5.5.7;13.7 Signalling Pathways and Sumoylation/Apoptosis;226
5.5.8;13.8 Conclusion;229
5.5.9;References;229
6;Part III Diseases;232
6.1;14 The Role of Sumoylation in Neurodegenerative Diseases;233
6.1.1;14.1 Introduction;233
6.1.2;14.2 Parkinsons Disease;234
6.1.3;14.3 Alzheimers Disease;236
6.1.4;14.4 Polyglutamine Diseases;237
6.1.4.1;14.4.1 Huntington's Disease;238
6.1.4.2;14.4.2 Denatorubro-Pallidoluysian Atrophy;238
6.1.4.3;14.4.3 Spinobulbar Muscular Atrophy;239
6.1.4.4;14.4.4 Spinocerebellar Ataxias;239
6.1.5;14.5 Neuronal Intranuclear Inclusion Disease;240
6.1.6;14.6 Cellular Stress;241
6.1.7;14.7 Ischemia;242
6.1.8;14.8 Sumoylation as a Potential Drug Target;243
6.1.9;14.9 Conclusions and Perspectives;246
6.1.10;References;247
6.2;15 Sumoylation and Its Contribution to Cancer;252
6.2.1;15.1 Introduction;252
6.2.2;15.2 Upstream Signals Regulating SUMO-Conjugation System in Cancer;253
6.2.3;15.3 Regulation of SUMO E2 Conjugating Enzyme, UBC9, in Cancer;255
6.2.4;15.4 Involvement of SUMO E3 Ligases in Cancer;256
6.2.5;15.5 Involvement of SUMO-Specific Proteases in Cancer;257
6.2.6;15.6 Regulation of Sumoylation at the Substrate Level and Implications in Cancer;258
6.2.7;15.7 SUMO Modification of Oncogenes and Tumor Suppressors;259
6.2.8;15.8 Conclusions;264
6.2.9;References;264
6.3;16 SUMO4-Encoded Genetic Susceptibility to Type 1 Diabetes;272
6.3.1;16.1 Introduction;273
6.3.2;16.2 Characterization of SUMO4 in T1D Susceptibility;274
6.3.3;16.3 Genetic Heterogeneity for SUMO4 in the European Caucasians;276
6.3.4;16.4 validation of SUMO4 as a Novel T1D Susceptibility Gene;277
6.3.5;16.5 The Effect of M55V Supports SUMO4 in T1D Susceptibility;280
6.3.6;16.6 Stress-Dependent SUMO4 Functionality;281
6.3.7;16.7 SUMO4 Acts as a Negative Regulator for the NFB Signaling Pathway;282
6.3.8;16.8 SUMO4 Regulates Cytokine-Initiated JAK/STAT Signaling;284
6.3.9;16.9 SUMO4 Modulates AP-1 Tanscriptional Activity;285
6.3.10;16.10 SUMO4 Wrestles with Intracellular Stress;287
6.3.11;16.11 Conclusions;289
6.3.12;References;289
6.4;17 Sumoylation in Craniofacial Disorders;299
6.4.1;17.1 Key Role for SUMO in Development;299
6.4.2;17.2 SUMO1 Haploinsufficiency Causes Cleft Lip and/or Palate;300
6.4.3;17.3 Sumoylation Regulates Craniofacial Developmental Genes;301
6.4.4;17.4 SUMO in Developmental Pathways and Syndromes;304
6.4.5;17.5 SUMO, Stress and CL/P;306
6.4.6;17.6 Conclusions;307
6.4.7;References;307
6.5;18 Viral Interplay with the Host Sumoylation System;312
6.5.1;18.1 Modification of Viral Proteins by Sumoylation;312
6.5.2;18.2 Viral Proteins that Affect Host Sumoylation;315
6.5.3;18.3 Herpes Simplex Virus;315
6.5.4;18.4 Cytomegalovirus;316
6.5.5;18.5 Human Herpesvirus 6;317
6.5.6;18.6 Epstein-Barr Virus;318
6.5.7;18.7 Adenovirus;318
6.5.8;18.8 Human Papillomavirus;320
6.5.9;18.9 Conclusion;322
6.5.10;References;323
6.6;Index;327