Ubiquitin and the biology of the cell:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
New York [u.a.]
Plenum Press
1998
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XX, 472 S. Ill., graph. Darst. |
| ISBN: | 0306456494 |
Internformat
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| 300 | |a XX, 472 S. |b Ill., graph. Darst. | ||
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| adam_text | Contents
Chapter 1
The Ubiquitin System: Past, Present, and Future Perspectives
Avram Hershko
1. Introduction 1
2. Discovery of the Role of Ubiquitin in Protein Breakdown 2
3. Identification of the Enzymatic Reactions of the Ubiquitin Pathway 3
4. Current State of Knowledge on Mechanisms and Functions
of the Ubiquitin System 5
4.1. Enzyme Components 5
4.2. Some Cellular Proteins Degraded by the Ubiquitin System . . 7
5. Challenges for the Future 11
6. Concluding Remarks 13
7. References 13
Chapter 2
Polyubiquitin Chains
Cecile M. Pickart
1. Introduction 19
2. Ubiquitin 20
2.1. Ubiquitin Conservation and Structure 20
2.2. Ubiquitin Genes 22
2.3. Ubiquitin Related Genes/Proteins 23
2.4. Ubiquitin Mutants 30
xi
xii • Contents
2.5. Chemically Modified Ubiquitin 36
2.6. Detection of Ubiquitination 38
3. Proteolytic Targeting Mediated by K48 Linked Poly ubiquitin
Chains 40
3.1. Existence and Significance of Targeting by K48 Linked
Chains 40
3.2. Chain Recognition Determinants 44
3.3. Metabolism of K48 Linked Chains 49
4. Other Polyubiquitin Chains 52
5. Concluding Remarks 56
6. References 57
Chapter 3
The Ubiquitin Conjugation System
Martin Scheffner, Susan Smith, and Stefan Jentsch
1. Introduction 65
2. Structure and Significance of Ubiquitin Protein Conjugates 66
3. Basic Enzymes of the Ubiquitin Conjugation System 67
3.1. Organization of the Ubiquitin Conjugation System 67
3.2. El, Ubiquitin Activating Enzymes 69
3.3. E2, Ubiquitin Conjugating Enzymes 72
3.4. E3, Ubiquitin Protein Ligases 80
4. Substrate Recognition, Specificity, and Regulation 84
4.1. Basic Concept of Substrate Recognition 84
4.2. Ubiquitination Signals 86
4.3. Ancillary Factors 88
4.4. Regulation 89
5. Perspective 90
6. References 91
Chapter 4
The Deubiquitinating Enzymes
Keith D. Wilkinson and Mark Hochstrasser
1. Introduction 99
2. Ubiquitin and Polyubiquitin Chains 100
2.1. Ubiquitin Precursors 100
2.2. Polyubiquitin Chains 101
I
Contents • xiii
2.3. Nonproductive Derivatives of Ubiquitin 102
2.4. Structural Features of Polymeric Ubiquitin 102
3. The Deubiquitinating Enzyme Families 103
4. General Characteristics of the Deubiquitinating Enzymes 105
! 5. Potential Roles for UBPs and UCHs 106
: 5.1. Processing of Ubiquitin Precursors 107
5.2. Recycling of Adventitiously Trapped Catalytic Intermediates 107
5.3. Proofreading of Protein Ubiquitination 108
i 5.4. Recycling of Ubiquitin from Polyubiquitinated Proteins
I following Commitment to Degradation 109
5.5. Maintaining Free Ubiquitin Levels and Keeping Proteasomes
Free of Ubiquitin Chains 11°
6. Analysis of Specific Deubiquitinating Enzymes 110
6.1. The UCH Family 11°
6.2. The UBP Family 114
7. Conclusions and Future Directions 120
; 8. References 120
Chapter 5
The 20 S Proteasome
Andrei Lupas and Wolfgang Baumeister
1. Introduction 127
2. Quaternary Structure 130
3. Secondary and Tertiary Structure I34
4. Mechanism ^
5. Substrate Specificity I39
6. Processing and Assembly I4
7. Concluding Remarks 142
8. References 143
Chapter 6
The 26 S Proteasome
Martin Rechsteiner
1. Introduction 147
2. Electron Microscopic Images of the 26 S Proteasome 149
3. The Proteasome 15l
3.1. C Terminal Extensions 151
xiv • Contents
3.2. On the Nature of Proteasome Active Sites 154
4. Regulatory Complex 156
4.1. Conjugate Degrading Factors 156
4.2. Naming Subunits of the Regulatory Complex 156
4.3. The ATPases 157
4.4. Non ATPase Subunits 161
4.5. Activities of the Regulatory Complex 165
4.6. The Regulatory Complex as a Polypeptide Pump 169
5. Assembly of the 26 S Proteasome 170
5.1. In Vitro Studies 170
5.2. In Vivo Studies 171
5.3. Dynamics of the 26 S Proteasome: Ribosome versus Solid
State Models 171
5.4. Subcomponents of the Regulatory Complex 171
5.5. One 26 S Proteasome or Many? 173
6. Substrate Recognition by the 26 S Proteasome 174
6.1. Widespread Occurrence of Substrates 174
6.2. Ubiquitin Dependence 174
6.3. The Role of Ubiquitin in Substrate Recognition 175
6.4. Polyubiquitin Chains Are Not Sufficient Degradation Signals 176
6.5. Recognition of Polyubiquitin Chains by the 26 S Proteasome 177
7. Intracellular Localization of Proteasomes and the 26 S Proteasome 178
7.1. Light Microscopic Analyses 178
7.2. Ultrastructural Studies 180
7.3. Signals for Nuclear Import 180
8. Summary and Perspectives 181
9. References 181
Chapter 7
Function of the Proteasome in Antigen Presentation
Jochen Beninga and Alfred L. Goldberg
1. Introduction 191
2. The Two Pathways for Antigen Presentation 191
3. Protein Ubiquitination and MHC Class I Presentation 194
4. Influence of the Rate of Ubiquitin Dependent Degradation on
Antigen Presentation 195
5. Selective Inhibitors of Proteasome Activity 197
6. Blocking Proteasome Function Prevents Antigen Presentation 199
Contents • xv
7. Regulation of Proteasome Composition by y Interferon 201
8. Biochemical Effects of the y Interferon Induced Subunits 202
9. Specific Functions of LMP2, LMP7, and the Homologous
Subunits 205
10. Immunological Significance of the Changes in Peptidase Activity 207
11. Involvement of the PA28 Activator in Antigen Presentation 211
12. Involvement of Other Cytosolic Proteases in Class I Processing .. 213
13. Conclusions 215
14. References 216
Chapter 8
The N End Rule Pathway
A. Varshavsky, C. Byrd, I. V. Davydov, R.J. Dohmen, F. Du,
M. Ghislain, M. Gonzalez, S. Grigoryev, E. S. Johnson, N. Johnsson,
J. A. Johnston, Y. T. Kwon, F. Levy, O. Lomovskaya, K. Madura,
I. Ota, T. Riimenapf, T. E. Shrader, T. Suzuki, G. Turner,
P. R. H. Waller, A. Webster, and Y. Xie
1. Introduction 224
2. Design, Components, and Evolution of the N End Rule Pathway 225
2.1. Definition of Terms 225
2.2. N Recognin (E3) 229
2.3. N Terminal Amidases 233
2.4. Aminoacyl tRNA Protein Transferases 236
2.5. Ubiquitin Conjugating Enzymes 237
2.6. The N End Rule as a Witness of Evolution 239
2.7. Code versus Hardware 240
3. Targeting Complex of the N End Rule Pathway 241
4. The N Degron and Pre N Degron 243
5. Mechanics of the N Degron 247
5.1. Stochastic Capture Model 247
5.2. cis trans Recognition and Subunit Specific Degradation of
Oligomeric Proteins 251
5.3. The Hairpin Insertion Model and the Function of
Multiubiquitin Chain 252
5.4. The N End Rule without Ubiquitin 253
6. Substrates and Functions of the N End Rule Pathway 254
6.1. Phenotypes of Mutants that Lack the N End Rule Pathway 254
6.2. The N End Rule Pathway and Osmoregulation in Yeast .... 255
xvi • Contents
6.3. The N End Rule Pathway and Import of Peptides in Yeast 255
6.4. On a Possible Function of the N End Rule Pathway
in Apoptosis 250
6.5. The N End Rule Pathway and Clostridial Neurotoxins 258
6.6. Ga Subunit of G Protein 260
6.7. Sindbis Virus RNA Polymerase 261
6.8. c Mos, a Proto Oncoprotein 262
6.9. Potential N End Rule Substrates 263
7. Determining the N End Rule and Probing the Kinetics of in Vivo
Protein Degradation 266
7.1. The UPR Technique 266
7.2. UPR and the Problem of Cotranslational Proteolysis 267
8. Applications of the N Degron 269
8.1. The N Degron and Conditional Mutants 269
8.2. The N Degron and Conditional Toxins 270
9. Epilogue 271
10. References 272
Chapter 9
Ubiquitin Dependent Degradation of Transcription Regulators
Mark Hochstrasser and Daniel Kornitzer
1. Introduction 279
2. Evidence Linking the Ubiquitin Pathway to the Degradation
of Specific Transcription Factors 280
2.1. Mata2 281
2.2. Gcn4 284
2.3. AP 1 285
2.4. MyoD 287
3. Degradation Signals 287
3.1. Recognition Sites 288
3.2. Ubiquitination Sites 291
4. Regulation of Degradation 293
4.1. p53 293
4.2. IkB 294
4.3. c Fos 294
4.4. Gcn4 295
4.5. MATa2 295
5. Concluding Remarks 297
6. References 298
!
; Contents • xvii
Chapter 10
Role of the Ubiquitin Proteasome Pathway in NF kB Activation
¦¦ Zhijian J. Chen and Tom Maniatis
1. Introduction 303
i 2. Role of Ubiquitin Proteasome Pathway in pi05 Processing 306
3. Signal Dependent Phosphorylation and Degradation of IkBci 309
j 4. Signal Dependent Ubiquitination of IkBqi 312
j 5. Enzymes Involved in the Phosphorylation and Ubiquitination
i oflKBa 313
! 5.1. Ubiquitination Enzymes 313
: 5.2. A Ubiquitination Dependent IkB Kinase 313
6. Basal Phosphorylation and Degradation of IkBoc 315
7. Signal Induced Degradation of Other IkB Proteins 316
7.1. IkBB 316
7.2. Cactus 316
8. Conclusions and Perspectives 317
9. References 318
Chapter 11
Ubiquitination of the p53 Tumor Suppressor
Jon M. Huibregtse, Carl G. Maki, and Peter M. Howley
1. E6 Dependent Ubiquitination of p53 324
1.1. The E6 Oncoprotein 324
1.2. E6 AP and the Ubiquitination of p53 327
1.3. The E6 AP Related Family of E3 Proteins 330
1.4. Structure Function Analyses of E6 and p53 334
2. E6 Independent Ubiquitination of p53 336
3. Remaining Questions 337
4. References 339
Chapter 12
Cell Cycle Control by Ubiquitin Dependent Proteolysis
Jan Michael Peters, Randall W. King, and Raymond J. Deshaies
1. Introduction 345
xviii • Contents
2. The Role of Ubiquitin Dependent Proteolysis in the Gl/S
Transition 346
2.1. Physiology and Biochemistry of the CDC34 Pathway 348
2.2. Regulation of CX C54 Dependent Ubiquitination 352
2.3. Recognition of Substrates by the CDC34 Pathway 355
2.4. Conservation of CDC34 Pathway Function 357
2.5. Links between Ubiquitin Dependent Proteolysis and the
Control of Gl Phase in Vertebrate Cells 359
3. Ubiquitin Dependent Proteolysis in Mitosis 359
3.1. Mitotic Cyclin Degradation 360
3.2. Chromosome Segregation 369
3.3. Other Proteins Degraded in Mitosis 371
3.4. Regulation of APC Dependent Ubiquitination 373
4. Perspectives 377
5. References 378
Chapter 13
Ubiquitination of Integral Membrane Proteins and Proteins
in the Secretory Pathway
Ron R. Kopito
1. Introduction 389
2. Quality Control and Protein Degradation Associated with the ER . . 390
2.1. Role of the Ubiquitin Proteasome Pathway in the
Degradation of Integral Membrane Proteins 391
2.2. Role of the Ubiquitin Proteasome Pathway in the
Degradation of Luminal (Secretory) Proteins 393
2.3. Is the Cytosolic Ubiquitin Proteasome Pathway the Major
Route for ER Degradation of Proteins? 395
2.4. Cytoplasmic Degradation of Membrane and Secretory
Proteins 396
3. The Role of Membrane Protein Ubiquitination in Cell Surface
Signaling 399
3.1. Ligand Induced Ubiquitination of Receptor Tyrosine Kinases 399
3.2. Ubiquitin and the Endocytic Pathway 402
3.3. Ubiquitin as a Versatile Protein Modification in Cellular
Protein Traffic 403
4. Summary of Prospects 404
5. References 405
Contents • xix
Chapter 14
Degradation of Ornithine Decarboxylase
Philip Coffino
1. Ornithine Decarboxylase and Its Products 411
2. Feedback Regulation Acts through Antizyme 412
3. Polyamines Control ODC Turnover 412
4. Distinct Elements of ODC Control Basal and Regulated
Degradation 413
5. Induction of Conformational Change in ODC by AZ 417
6. Domains of AZ Required for ODC Binding and Degradation .... 419
7. Ubiquitin System Not Involved in AZ Regulated Degradation .... 419
8. Function of AZ in Degradation 421
9. Conservation of Regulation of ODC 423
10. Why Not Ubiquitin? 423
11. References 424
Chapter 15
Ubiquitin and the Molecular Pathology of Human Disease
R. John Mayer, Michael Landon, and James Lowe
1. Introduction 429
1.1. Disorders Involving the Ubiquitin System 430
1.2. Probes Used in the Study of Ubiquitin in Human Disease . . 430
2. Ubiquitin in Chronic Degenerative Diseases 432
2.1. Ubiquitin and the Normal Endosome Lysosome System . . . 433
2.2. Disease Related Lysosomal Accumulation of Ubiquitin .... 434
2.3. Ubiquitin and the Role of Endosomes and Lysosomes in
Disease Pathogenesis 435
2.4. Inclusion Bodies in Neurodegenerative Diseases 436
2.5. Ubiquitin Accumulation in Nerve Cell Processes 441
2.6. Proposed Generalized Role for Ubiquitin in
Neurodegenerative Disease 445
3. Ubiquitin in Acute Cell Injury: The Cell Stress Response 446
3.1. Ischemia 446
3.2. Oxidative Stress 447
4. Ubiquitin Involvement in Cell Atrophy and Programmed Cell
Death 448
4.1. Skeletal Muscle Atrophy 448
xx • Contents
4.2. Programmed Cell Death 450
5. Summary 451
6. References 452
Index 463
|
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| spelling | Ubiquitin and the biology of the cell ed. by Jan-Michael Peters ... New York [u.a.] Plenum Press 1998 XX, 472 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd rswk-swf Intrazellulärraum (DE-588)4330337-7 gnd rswk-swf Proteolyse (DE-588)4047534-7 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Ubiquitin (DE-588)4314848-7 s Proteolyse (DE-588)4047534-7 s Intrazellulärraum (DE-588)4330337-7 s DE-604 Peters, Jan-Michael Sonstige oth HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008196683&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Ubiquitin and the biology of the cell Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd Intrazellulärraum (DE-588)4330337-7 gnd Proteolyse (DE-588)4047534-7 gnd |
| subject_GND | (DE-588)4314848-7 (DE-588)4330337-7 (DE-588)4047534-7 (DE-588)4143413-4 |
| title | Ubiquitin and the biology of the cell |
| title_auth | Ubiquitin and the biology of the cell |
| title_exact_search | Ubiquitin and the biology of the cell |
| title_full | Ubiquitin and the biology of the cell ed. by Jan-Michael Peters ... |
| title_fullStr | Ubiquitin and the biology of the cell ed. by Jan-Michael Peters ... |
| title_full_unstemmed | Ubiquitin and the biology of the cell ed. by Jan-Michael Peters ... |
| title_short | Ubiquitin and the biology of the cell |
| title_sort | ubiquitin and the biology of the cell |
| topic | Ubiquitin Ubiquitins Ubiquitin (DE-588)4314848-7 gnd Intrazellulärraum (DE-588)4330337-7 gnd Proteolyse (DE-588)4047534-7 gnd |
| topic_facet | Ubiquitin Ubiquitins Intrazellulärraum Proteolyse Aufsatzsammlung |
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