The articles in this book are focused on the modifiers ubiquitin, SUMO1/2/3, NED 8, ISG15 and FAT10. They discuss how conjugation enzymes determine specific linkages and how they are interpreted by ubiquitin binding domains.
_ 1 a a 4 _ 17 10 15 ubiquitin; and of 16 VCP 17 18 20 33 34 34 36 p domain. 41 42 42 43 P U 42 47 binding. C. elegans 16 In 21 22 50 51 52 53 13 and UFD 4 10 of Cdc48. 18 30 of Ufd2. COFACTORS 47 23 13 47 47 47 72 15 15 and of Spt23 p90. Ufd2 and Cdc48. In C. elegans 74 16 75 75 76 76 Ufd2 25 54 54 7 56 p47 7 7 80 30 30 81 82 82 but and CD3 26 DUB COFACTORS 30 UFD3 OTU1 4 Cdc48 30 4 OLE1. 15 27 87 REFERENCES 30 REGULATION OF UBIQUITIN MONOUBIQUITINATION UBIQUITINATION 1 32 7 S) d 33 12 13 14 15 18 19 15 20 21 35 15 15 27 15 31 32 31 33 36 monoubiquitination of pol pol 34 37 34 monoubiquitination. 20 35 trans 3 15 REFERENCES by monoubiquitination. Mol Cell; 2009. UBIQUITIN LIGASE ACTIVITY BY Nedd 1 2 of 41 5 6 8 fold. 9 13 14 edd 43 18 18 K M and k 18 22 23 K M 24 25 K M 26 edd 45 18 27 K M K D 18 25 . 8 10 M 21 28 MECHANISM AND REGULATION OF CRLs 34 41 34 edd 47 48 S. pombe 49 51 p27 and I by SCF and SCF 57 58 59 60 CTD CTD CTD CTD in Cul5 CTD CTD CTD 60 18
Preface: New Paradigms in the Conjugation of Ubiquitin Family Modifiers xvii
Marcus Groettrup
1. Activation of Ubiquitin and Ubiquitin?Like Proteins 1
Frederick C. Streich, Jr. and Arthur L. Haas
2. Control of Ubiquitin Conjugation by Cdc48 and Its Cofactors 17
Alexander Buchberger
3. Regulation of Ubiquitin Receptors by Coupled Monoubiquitination 31
Daniela Hoeller and Ivan Dikic
4. Control of Cullin?Ring Ubiquitin Ligase Activity by Nedd8 41
Raymond J. Deshaies, Ethan D. Emberley and Anjanabha Saha
5. Control of Deneddylation by the Cop9 Signalosome 57
Tilo Schmaler and Wolfgang Dubiel
6. Mechanism, Specificity and Structure of the Deubiquitinases 69
David Komander
7. Ubiquitin Conjugation and Deconjugation in NF?kB Signaling 88
Michael Düwel, Kamyar Hadian and Daniel Krappmann
8. Functions of Linear Ubiquitin Chains in the NF?kB Pathway: Linear Polyubiquitin in NF??B Signaling 100
Kazuhiro Iwai
9. Assembly of K11?Linked Ubiquitin Chains by the Anaphase?Promoting Complex 107
Michael Rape
10. Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53 116
Dimitris P. Xirodimas and Martin Scheffner
11. Ubiquitylation in the ERAD Pathway 136
Frederik Eisele, Antje Schäfer and Dieter H. Wolf
12. Pupylation: A Signal for Proteasomal Degradation in Mycobacterium tuberculosis 149
Kristin E. Burns and K. Heran Darwin
13. sumo Control 158
Katharina Maderböck and Andrea Pichler
14. The In Vivo Functions of Desumoylating Enzymes 170
Tasneem Bawa?Khalfe and Edward T.H. Yeh15. Regulatory Functions of Ubiquitin and Sumo in DNA Repair Pathways 184
Stefan Jentsch and Stefan Müller
16. Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation 195
Maria Miteva, Kirstin Keusekotten, Kay Hofmann, Gerrit J.K. Praefcke and R. Jürgen Dohmen
17. In Vivo Functions of Isgylation 215
Klaus?Peter Knobeloch
18. Identification and Validation of ISG15 Target Proteins 228
Larissa A. Durfee and Jon M. Huibregtse
19. FAT 10: Activated by UBA6and Functioning in Protein Degradation 238
Christiane Pelzer and Marcus Groettrup
Index 247
1
Über den Autor
MARCUS GROETTRUP is a Professor for Immunology in the Department of
Biology of Konstanz University in Germany. His main interests are in the role of the immunoproteasome in antigen fragmentation and autoimmunity. Moreover, he has studied the function and conjugation of the ubiquitin-like protein FAT10. He studied biochemistry in Tübingen and ET H Zürich and did his diploma thesis in the laboratory of H. Hengartner and R. Zinkernagel. During his PhD at the Basel Institute for Immunology with H. von Boehmer he discovered the pre T cell receptor. After habilitation at Humboldt University Berlin in the group of P-M. Kloetzel on the topic of antigen processing he founded his own group at the Cantonal Hospital St. Gallen, Switzerland. Since 2002 he holds the Chair of Immunology at the University of Konstanz, Germany. Several prizes were awarded to Dr. Groettrup like the Award of the Sandoz Foundation for Therapeutic Research, the Karl Lohmann Prize of the German Society for Biological Chemistry, the Langener Science Prize of the Paul Ehrlich Institute, and the Research Award by the CaP CURE foundation.
Inhaltsverzeichnis
Preface: New Paradigms in the Conjugation of Ubiquitin Family Modifiers xvii
Marcus Groettrup
1. Activation of Ubiquitin and Ubiquitin?Like Proteins 1
Frederick C. Streich, Jr. and Arthur L. Haas
2. Control of Ubiquitin Conjugation by Cdc48 and Its Cofactors 17
Alexander Buchberger
3. Regulation of Ubiquitin Receptors by Coupled Monoubiquitination 31
Daniela Hoeller and Ivan Dikic
4. Control of Cullin?Ring Ubiquitin Ligase Activity by Nedd8 41
Raymond J. Deshaies, Ethan D. Emberley and Anjanabha Saha
5. Control of Deneddylation by the Cop9 Signalosome 57
Tilo Schmaler and Wolfgang Dubiel
6. Mechanism, Specificity and Structure of the Deubiquitinases 69
David Komander
7. Ubiquitin Conjugation and Deconjugation in NF?kB Signaling 88
Michael Düwel, Kamyar Hadian and Daniel Krappmann
8. Functions of Linear Ubiquitin Chains in the NF?kB Pathway: Linear Polyubiquitin in NF??B Signaling 100
Kazuhiro Iwai
9. Assembly of K11?Linked Ubiquitin Chains by the Anaphase?Promoting Complex 107
Michael Rape
10. Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53 116
Dimitris P. Xirodimas and Martin Scheffner
11. Ubiquitylation in the ERAD Pathway 136
Frederik Eisele, Antje Schäfer and Dieter H. Wolf
12. Pupylation: A Signal for Proteasomal Degradation in Mycobacterium tuberculosis 149
Kristin E. Burns and K. Heran Darwin
13. sumo Control 158
Katharina Maderböck and Andrea Pichler
14. The In Vivo Functions of Desumoylating Enzymes 170
Tasneem Bawa?Khalfe and Edward T.H. Yeh
15. Regulatory Functions of Ubiquitin and Sumo in DNA Repair Pathways 184
Stefan Jentsch and Stefan Müller
16. Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation 195
Maria Miteva, Kirstin Keusekotten, Kay Hofmann, Gerrit J.K. Praefcke and R. Jürgen Dohmen
17. In Vivo Functions of Isgylation 215
Klaus?Peter Knobeloch
18. Identification and Validation of ISG15 Target Proteins 228
Larissa A. Durfee and Jon M. Huibregtse
19. FAT 10: Activated by UBA6and Functioning in Protein Degradation 238
Christiane Pelzer and Marcus Groettrup
Index 247
Klappentext
+ 1 a a 4 + 17 10 15 ubiquitin; and of 16 VCP 17 18 20 33 34 34 36 p domain. 41 42 42 43 P U 42 47 binding. C. elegans 16 In 21 22 50 51 52 53 13 and UFD 4 10 of Cdc48. 18 30 of Ufd2. COFACTORS 47 23 13 47 47 47 72 15 15 and of Spt23 p90. Ufd2 and Cdc48. In C. elegans 74 16 75 75 76 76 Ufd2 25 54 54 7 56 p47 7 7 80 30 30 81 82 82 but and CD3 26 DUB COFACTORS 30 UFD3 OTU1 4 Cdc48 30 4 OLE1. 15 27 87 REFERENCES 30 REGULATION OF UBIQUITIN MONOUBIQUITINATION UBIQUITINATION 1 32 7 S) d 33 12 13 14 15 18 19 15 20 21 35 15 15 27 15 31 32 31 33 36 monoubiquitination of pol pol 34 37 34 monoubiquitination. 20 35 trans 3 15 REFERENCES by monoubiquitination. Mol Cell; 2009. UBIQUITIN LIGASE ACTIVITY BY Nedd 1 2 of 41 5 6 8 fold. 9 13 14 edd 43 18 18 K M and k 18 22 23 K M 24 25 K M 26 edd 45 18 27 K M K D 18 25 . 8 10 M 21 28 MECHANISM AND REGULATION OF CRLs 34 41 34 edd 47 48 S. pombe 49 51 p27 and I by SCF and SCF 57 58 59 60 CTD CTD CTD CTD in Cul5 CTD CTD CTD 60 18
Focussed on the modifiers ubiquitin, SUMO1/2/3, NED 8, ISG15 and FAT10
Discusses how conjugation enzymes determine specific linkages and how they are interpreted by ubiquitin binding domains
Cross-talk between the ubiquitin family modification systems
