Conjugation and Deconjugation of Ubiquitin Family Modifiers (Subcellular Biochemistry, 54)

To cope with the steadily growing body of knowledge and for organizational reasons the articles in this book are focussed on the modifiers ubiquitin, SUMO1/2/3, NED 8, ISG15 and FAT10 but it should be at least mentioned here that enzymes involved in conjugation and deconjugation of URM1, UFM1, ATG8 and ATG12 have been reported and continue to be investigated. Content: Front Matter....Pages i-xx Activation of Ubiquitin and Ubiquitin-Like Proteins....Pages 1-16 Control of Ubiquitin Conjugation by Cdc48 and Its Cofactors....Pages 17-30 Regulation of Ubiquitin Receptors by Coupled Monoubiquitination....Pages 31-40 Control of Cullin-Ring Ubiquitin Ligase Activity by Nedd8....Pages 41-56 Control of Deneddylation by the COP9 Signalosome....Pages 57-68 Mechanism, Specificity and Structure of the Deubiquitinases....Pages 69-87 Ubiquitin Conjugation and Deconjugation in NF-κB Signaling....Pages 88-99 Functions of Linear Ubiquitin Chains in the NF-κB Pathway....Pages 100-106 Assembly of K11-Linked Ubiquitin Chains by the Anaphase-Promoting Complex....Pages 107-115 Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53....Pages 116-135 Ubiquitylation in the ERAD Pathway....Pages 136-148 Pupylation....Pages 149-157 Sumo Control....Pages 158-169 The In Vivo Functions of Desumoylating Enzymes....Pages 170-183 Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways....Pages 184-194 Sumoylation as a Signal for Polyubiquitylation and Proteasomal Degradation....Pages 195-214 In Vivo Functions of Isgylation....Pages 215-227 Identification and Validation of ISG15 Target Proteins....Pages 228-237 FAT10....Pages 238-246 Back Matter....Pages 247-252 The conjugation of ubiquitin and ubiquitin-like modifiers by activating enzymes (E1), conjugating enzymes (E2) and ligases (E3) has been a subject of intensive research in the past years. The complexity of the conjugation cascades with dozens of E2 enzymes and hundreds of E3 enzymes requires that emerging common principles are delineated. On the other hand the functional implications for each modifier need to be considered. In this book leading experts actively investigating the conjugation and deconjugation enzymes for ubiquitin, SUMO, NEDD8, ISG15 and FAT10 review the progress in the specific fields. Moreover, novel insights into the function of the respective modifiers are presented. This book should allow scientists from all areas of cell biology and molecular medicine as well as students and young scientists entering this field to get an introduction to ubiquitin modifier conjugation and to get an update on recent insights into this intensively investigated area of research. --Book Jacket † 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