GTPases:
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Oxford [u.a.]
Oxford Univ. Press
2000
|
| Schriftenreihe: | Frontiers in molecular biology
24 |
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XIX, 340 S. Ill., graph. Darst. |
| ISBN: | 0199637458 019963744X |
Internformat
MARC
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| 245 | 1 | 0 | |a GTPases |c ed. by Alan Hall |
| 264 | 1 | |a Oxford [u.a.] |b Oxford Univ. Press |c 2000 | |
| 300 | |a XIX, 340 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
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| 490 | 1 | |a Frontiers in molecular biology |v 24 | |
| 650 | 4 | |a Enzymes |x Analysis | |
| 650 | 4 | |a Guanosine triphosphatase | |
| 650 | 4 | |a Guanosine triphosphatase |x Biotechnology | |
| 650 | 4 | |a Guanosine triphosphate | |
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Datensatz im Suchindex
| _version_ | 1804127721481043968 |
|---|---|
| adam_text | Contents
Preface
ALAN HALL
List of contributors xv
Abbreviations xvii
1 G proteins I: Gs and Gj 1
SUSANNE M. MUMBY
1. Introduction: from pheromones to photons 1
1.1 In the beginning ... 1
1.2 G protein diversity 3
1.3 Mechanistic model 4
2. Covalent modifications of a subunits 6
2.1 ADP ribosylation 6
2.2 Acylation 8
3. Targets 9
3.1 Adenylyl cyclases 10
3.2 Light activated cGMP phosphodiesterase 12
3.3 Ion channels 13
3.4 Other targets of Gp^ 13
4. Regulation of signalling by G APs 17
4.1 Effectors as GAPs 18
4.2 RGS proteins as G APs 18
5. Organization 19
6. Genetic analysis 21
6.1 as 21
6.2 a,, 22
6.3 a() 23
7. Disease in humans caused by defects in G proteins 24
7.1 Bacterial toxins 24
7.2 Genetic mutations 25
viii CONTENTS
27
Acknowledgements
27
References
2 G proteins II: Gq, G12, and Gz 35
JENNIFER L. GLICK, THOMAS E. MEIGS, AND PATRICK J. CASEY
1. Introduction 35
2. Covalent modifications of PTX resistant G proteins 37
2.1 Lipid modifications of G proteins 37
2.2 Phosphorylation of G proteins 41
3. Signalling through Gq proteins *3
3.1 Regulation of phosphoinositide specific phospholipase C activity 43
3.2 Genetic studies on the Gq subfamily *4
4. Signalling through G12 proteins *5
4.1 Biological consequences of activating G12 proteins 4j
4.2 Genetic studies on the G12 subfamily **
5. Signalling through Gza 49
6. Regulation of signal termination ^
6.1 Effectors of G proteins as GAPs
6.2 RGS proteins 53
7. Concluding remarks ^
References 56
3 Ras 67
JOHANNES L. BOS
1. Introduction 67
2. Background 67
2.1 Ras is the product of proto oncogenes ^
2.2 Ras is involved in signal transduction 69
3. Biochemical properties of Ras 70
4. Regulation of Ras activity 71
4.1 Guanine nucleotide exchange factors (GEFs) 71
4.2 GTPase activating proteins (GAPs) 71
5. Effectors of Ras 73
5.1 The serine threonine kinases of the Raf family ^3
CONTENTS j ix
5.2 The pi 10 catalytic subunit of phosphatidylinositol 3 kinase 73
5.3 Ral guanine nucleotide exchange factors (RalGEFs) 74
5.4 Other effectors 74
6. Biological responses 74
6.1 Oncogenic Ras induces proliferation and differentiation 74
6.2 Function of endogenous Ras 75
7. Ras in lower eukaryotes 76
7.1 Ras in vulva development in C. elegans 76
7.2 Ras in eye development in Drosophila 78
7.3 Ras in yeast 78
8. Other Ras like GTPases 79
8.1 Ral 79
8.2 Rapl 80
8.3 Rap2 81
8.4 R ras 82
8.5 TC21 82
8.6 Rheb 82
9. Conclusions 82
Acknowledgement 83
References 83
4 Rho 89
ANNE J. RIDLEY
1. Introduction 89
2. Structure and expression of Rho GTPases 89
2.1 Sequence and structure 89
2.2 Post translational modifications 92
2.3 Expression of Rho GTPases 93
3. Mechanisms of activating and inactivating Rho GTPases 93
3.1 Nucleotide exchange and exchange factors 94
3.2 GTP hydrolysis and GAPs 96
3.3 GDIs 97
4. Downstream interacting proteins 98
4.1 Rho targets 98
4.2 Rac and Cdc42 targets 99
5. Rho GTPases and the actin cytoskeleton 101
x CONTENTS
5.1 Rho 101
5.2 Rac and Cdc42 104
5.3 Rho and Cdc42 in cytokinesis 109
5.4 Other Rho GTPases n0
6. Rho GTPases and cell adhesion m
6.1 Adhesion to the extracellular matrix m
6.2 Intercellular adhesions H2
7. Rho GTPases, cell polarity, and cell migration 113
8. Regulation of transcription, cell cycle, and transformation 114
8.1 Rho proteins in oncogenic transformation H4
8.2 Transcriptional regulation and links with cell cycle control 115
9. Other activities of Rho GTPases li7
9.1 Activation of the NADPH oxidase H7
9.2 Phagocytosis and entry of bacteria into cells H
11
9.3 Secretion and endocytosis 11D
10. Conclusions li9
References H
5 Rab 137
RUTH N. COLLINS AND PATRICK BRENNWALD
1. Introduction 137
1.1 Rabs in yeast 137
1.2 Rabs in mammals 13°
1.3 Rabs in other organisms
1.4 Evolutionary conservation of Rab function 1
1.5 Functional specificity of Rab proteins 1
2. Post translational modification I42
2.1 Prenylation 142
2.2 Phosphorylation 143
3. Cellular localization I43
4. Biochemistry of point mutants 146
5. Models for Rab protein function I47
6. Genetic analysis of Rab function 150
6.1 Yeast I50
6.2 Metazoan organisms 1^
7. Cellular assays of Rab function 152
CONTENTS | xi
8. Accessory factors 152
8.1 GDI 152
8.2 Exchange factors 153
8.3 GAP proteins 155
8.4 Effector molecules 157
9. Outstanding questions 163
9.1 Identification of novel Rab protein regulators 163
9.2 Roles of lipid modification 163
9.3 How do Rabs communicate with the SNARE machinery? 164
9.4 Cross talk of Rab proteins with other signalling cascades? 164
9.5 Links between Rab proteins and the cytoskeleton 165
9.6 Rabs and lipid metabolism 165
9.7 Genetic studies of Rab function in metazoan organisms 165
10. Conclusions 165
Acknowledgements 166
References 166
6 Arf 176
MICHAEL G. ROTH
1. Introduction 176
2. The Arf family 176
3. Biochemical properties of Arf proteins 177
4. Cellular activities of Arf proteins 178
4.1 Arf function in yeast 179
4.2 Studies of Arf function in mammalian cells using reverse genetics 180
4.3 Studies using inhibitors in intact mammalian cells 181
4.4 In vitro assays with broken cells or isolated membranes 182
5. Arf GEF proteins 182
6. Arf GAP proteins 184
7. A revised model for guanine nucleotide exchange on Arf 186
8. Negative feedback regulation through Arf GAP 189
9. Sari 189
10. Conclusion 192
References 192
xii I CONTENTS
7 Ran 198
IAN G. MACARA, AMY BROWNAWELL, AND KATIE WELCH
1. Introduction 198
2. The Ran GTPase 198
3. Regulating the Ran GTPase cycle 200
3.1 RCC1 20°
3.2 RanGAP 201
4. The importing family of Ran binding proteins 202
5. The RanBD family of Ran binding proteins 204
5.1 RanBPl 205
5.2 RanBP2 206
5.3 RanBP3 207
6. NTF2/plO 208
7. Dis3 and other Ran binding proteins 2^
8. Ran and nucleocytoplasmic transport 2^
9. Conclusions 2
References 2^
8 GTPases in protein translocation and protein elongation 222
DOUGLAS M. FREYMANN AND PETER WALTER
1. Introduction 222
2. GTPases in SRP mediated protein targetting 22
3. GTPases in protein elongation 2
4. Conclusions 2^
References 2^
9 The functioning of molecular switches in
three dimensions 244
ALFRED WITTINGHOFER
1. Introduction 2^
2. General properties of GTP binding proteins 244
2.1 Biochemistry 244
CONTENTS i xiii
2.2 General features of the G domain 245
2.3 The sequence elements 247
3. Structures of small GTP binding proteins 249
3.1 Ras 249
3.2 RaplAandRap2 251
3.3 Arf 252
3.4 Ran 254
3.5 Cdc42/Rho/Rac 255
3.6 Rab 257
4. Heterotrimeric G proteins 257
4.1 a subunit structures 258
4.2 The conformational change 260
4.3 Ga subunits complexed to GDP and A1F4 261
4.4 Mutants of Gicd and the GDP Pi state 262
5. Guanine nucleotide dissociation inhibitors 263
5.1 RabGDI structure 263
5.2 RhoGDI structure 264
5.3 NTF2 and its complex with Ran*GDP 266
5.4 The P7 subunit and the heterotrimeric G protein 268
6. Guanine nucleotide exchange factors—GEFs 270
6.1 Mechanism and kinetics of GEFs 270
6.2 Mss4 272
6.3 Arf GEFs, the sec7 domain 272
6.4 RanGEF,RCCl 273
6.5 Rho GEFs, the DH domain 275
7. Complexes and structural mechanism 277
7.1 Ras Sos 277
7.2 The Sec7 Arf complex 278
7.3 A universal mechanism of GEF catalysed exchange? 279
7.4 Structural models for the receptor G protein exchange mechanism 280
8. The GTPase reaction and GTPase activating proteins—GAPs 281
8.1 Structures of Ras GAP and Rho GAP 282
8.2 The Ras Ras GAP complex 283
8.3 Rho Rho GAP complexes 284
8.4 Mechanism of GTPase activation: arginine finger crosses the GAP 286
8.5 A heterodimer enzyme 287
8.6 RGS proteins and the GIul RGS4 complex 287
9. Interactions with effectors 289
xiv I CONTENTS
9.1 Ras effectors 289
9.2 Structure of the Ras RafRBD complex 289
9.3 RasandRalGEF 291
9.4 Ran effectors 292
9.5 Structure of the Ran«GppNHp»RanBDl complex 292
9.6 Ga protein adenylyl cyclase interaction 29^
10. Concluding remarks 297
Acknowledgements 298
References 298
10 GTPases targetted by bacterial toxins 3ii
KLAUS AKTORIES, GUDULA SCHMIDT, AND FRED HOFMANN
1. Introduction 311
2. Diphtheria toxin and Pseudomonas aeruginosa exotoxin A: ADP
ribosylation of elongation factor 2 311
3. Toxins modifying heterotrimeric G proteins 313
4. C3 like ADP ribosyltransferases 313
4.1 ADP ribosylationofRho 314
5. Pseudomonas aeruginosa exoenzyme S 316
6. Large clostridial cytotoxins 318
6.1 Glucosylation of small GTPases 318
6.2 Structure activity relationship of large clostridial cytotoxins 319
7. Activation of Rho GTPases by bacterial toxins 321
7.1 Cytotoxic necrotizing factors, CNF1 and 2 321
7.2 Structure activity analysis of CNF 322
7.3 Dermonecrotizing toxin (DNT) 323
8. Concluding remarks 323
References 324
Index 332
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| id | DE-604.BV013025789 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T18:37:51Z |
| institution | BVB |
| isbn | 0199637458 019963744X |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-008873431 |
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| owner_facet | DE-12 DE-703 DE-355 DE-BY-UBR DE-11 |
| physical | XIX, 340 S. Ill., graph. Darst. |
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| publisher | Oxford Univ. Press |
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| series | Frontiers in molecular biology |
| series2 | Frontiers in molecular biology |
| spelling | GTPases ed. by Alan Hall Oxford [u.a.] Oxford Univ. Press 2000 XIX, 340 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Frontiers in molecular biology 24 Enzymes Analysis Guanosine triphosphatase Guanosine triphosphatase Biotechnology Guanosine triphosphate Biotechnologie (DE-588)4069491-4 gnd rswk-swf GTP-bindende Proteine (DE-588)4248354-2 gnd rswk-swf Guanosintriphosphatasen (DE-588)4324625-4 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Guanosintriphosphatasen (DE-588)4324625-4 s DE-604 Biotechnologie (DE-588)4069491-4 s GTP-bindende Proteine (DE-588)4248354-2 s Hall, Alan Sonstige oth Frontiers in molecular biology 24 (DE-604)BV010329078 24 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008873431&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | GTPases Frontiers in molecular biology Enzymes Analysis Guanosine triphosphatase Guanosine triphosphatase Biotechnology Guanosine triphosphate Biotechnologie (DE-588)4069491-4 gnd GTP-bindende Proteine (DE-588)4248354-2 gnd Guanosintriphosphatasen (DE-588)4324625-4 gnd |
| subject_GND | (DE-588)4069491-4 (DE-588)4248354-2 (DE-588)4324625-4 (DE-588)4143413-4 |
| title | GTPases |
| title_auth | GTPases |
| title_exact_search | GTPases |
| title_full | GTPases ed. by Alan Hall |
| title_fullStr | GTPases ed. by Alan Hall |
| title_full_unstemmed | GTPases ed. by Alan Hall |
| title_short | GTPases |
| title_sort | gtpases |
| topic | Enzymes Analysis Guanosine triphosphatase Guanosine triphosphatase Biotechnology Guanosine triphosphate Biotechnologie (DE-588)4069491-4 gnd GTP-bindende Proteine (DE-588)4248354-2 gnd Guanosintriphosphatasen (DE-588)4324625-4 gnd |
| topic_facet | Enzymes Analysis Guanosine triphosphatase Guanosine triphosphatase Biotechnology Guanosine triphosphate Biotechnologie GTP-bindende Proteine Guanosintriphosphatasen Aufsatzsammlung |
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