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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
List of contents
Activation of Ubiquitin and Ubiquitin-Like Proteins.- Control of Ubiquitin Conjugation by Cdc48 and Its Cofactors.- Regulation of Ubiquitin Receptors by Coupled Monoubiquitination.- Control of Cullin-Ring Ubiquitin Ligase Activity by Nedd8.- Control of Deneddylation by the COP9 Signalosome.- Mechanism, Specificity and Structure of the Deubiquitinases.- Ubiquitin Conjugation and Deconjugation in NF-?B Signaling.- Functions of Linear Ubiquitin Chains in the NF-?B Pathway.- Assembly of K11-Linked Ubiquitin Chains by the Anaphase-Promoting Complex.- Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53.- Ubiquitylation in the ERAD Pathway.- Pupylation.- Sumo Control.- The In Vivo Functions of Desumoylating Enzymes.- Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways.- Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation.- In Vivo Functions of Isgylation.- Identification and Validation of ISG15 Target Proteins.- FAT10.
About the author
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.
Summary
† 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
