The nuclear envelope:
Gespeichert in:
Format: | Buch |
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Sprache: | English |
Veröffentlicht: |
Abingdon, Oxon, OX, UK
BIOS Scientific Publishers
2004
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Schlagworte: | |
Online-Zugang: | Table of contents Inhaltsverzeichnis |
Beschreibung: | Includes bibliographical references and index |
Beschreibung: | xviii, 344 p. ill. (some col.) 24 cm |
ISBN: | 0415346452 |
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Datensatz im Suchindex
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adam_text | The Nuclear Envelope
Edited by
D E EVANS
Research School of Biological and Molecular Sciences, Oxford Brookes
University, Oxford, UK
C J HUTCHISON
Department of Biological Sciences, University of Durham, Durham, UK
J A BRYANT
Department of Biological Sciences, University of Exeter, Exeter, UK
O
( A BIOS Scientific Publishers
• ^ Taylor amp; Francis Croup
Contents
Contributors xv
Abbreviations xvii
Preface xix
1 The nuclear envelope: a comparative overview 1
David E Evans, John A Bryant and Chris Hutchison
A general description of the nuclear envelope 2
Nuclear envelope formation 2
Nuclear pore complexes and transport across the nuclear envelope 3
Nuclear lamina 4
Proteins of the nuclear envelope 5
Conclusion 7
References 7
2 The nuclear envelope proteome 9
Mathias Dreger and Henning Otto
Introduction 9
Structure of the nuclear envelope 10
Subcompartments of the nuclear envelope 10
Cell cycle dependence of the nuclear envelope structure 11
Analytical challenges in nuclear envelope proteomics 12
Strategies in nuclear envelope proteomics 12
Experimental approaches to subcellular proteomes 12
Protein identification techniques 15
Nuclear envelope proteomics 17
Proteins of the nuclear envelope 19
Outer nuclear membrane proteins 24
Proteins of the nuclear pore complex 25
Inner nuclear membrane proteins 26
Lamins 29
Proteins associated with inner nuclear membrane and lamina 30
Proteins putatively associated with the nuclear envelope 31
Post-translational modifications at the nuclear envelope 32
Conclusions 32
References 33
3 Nuclear envelope proteins and human disease 41
Howard J Worman
Nuclear envelope: overall structure 41
Integral proteins of the inner nuclear membrane of vertebrates 42
Nuclear lamina and the human nuclear lamin gene family 42
Invasion of the positional cloners 44
Mouse models of human diseases caused by nuclear envelope protein mutations 46
How do mutations in emerin and lamins A and C cause the same disease? 47
How do mutations in widely expressed proteins cause tissue-specific diseases? 47
viii CONTENTS
How do different mutations in lamins A and C cause different diseases? 49
Conclusions 49
References 50
4 Protein interactions, right or wrong, in Emery-Dreifuss muscular dystrophy 57
Glenn E Morris
Introduction 57
Nuclear foci of A-type lamins 58
Cell division, degeneration and death 61
Interactions of emerin and other proteins 62
Acknowledgements 65
References 65
5 Plant nuclear envelope proteins 69
Annkatrin Rose, Shalaka Patel and Iris Meier
Introduction 69
The plant nuclear envelope as scaffold for macromolecular complexes 69
Do plant cells have lamins? 69
A connection between the nuclear envelope and the actin cytoskeleton? 72
Microtubule nucleation at the plant nuclear envelope 72
Meiotic tethering of telomeres to the nuclear envelope 74
Targeting across and into the plant nuclear envelope 75
Gateways in the plant nuclear envelope 75
Nuclear import and export 76
The ran cycle in plants 77
Nuclear envelope targeting in plants 78
Signal transduction at the plant nuclear envelope 80
G proteins r 80
Ca2+ signalling 80
Proteasome-mediated proteolysis 81
Summary 81
Acknowledgements 82
References - 82
6 Structure, function and assembly of the nuclear pore complex 89
Sheona Drummond and Terry Allen
Introduction 89
NPC structure 90
Cytoplasmic filaments and cytoplasmic annular components 90
Nuclear pore membrane proteins 90
Central compartment of the NPC 92
Nucleoplasmic annular components 92
Nuclear pore basket and associated nucleoplasmic filaments 92
Annulate lemellae 92
Identification of the NPC proteome 93
FG-repeat, FXFG-repeat and GLFG-repeat nucleoporins 93
WD-repeat nucleoporins 94
Post-translation modifications of nucleoporins 95
NPC protein complexes and their functions 96
p62 complex 97
CONTENTS ix
Nupl07-160 complex and yeast nup84 complex 97
Nup93-nup205-nupl88 complex • 97
Nup98-nup88 and nup98-nup96 complexes 98
Nup88 complex 98
Traversing the nuclear pore 98
Transport-cargo chaperones and the Ran gradient 98
Translocation through the centre of the pore 99
Filamentous size exclusion model 99
Hydrophobic partitioning model 99
Affinity gradient model 101
NPC assembly 101
The molecular requirements for NPC assembly 102
Hierarchical recruitment of nups to the reforming nuclear envelope 102
The role of Ran in NPC assembly 104
Nucleoporins and disease 104
Nup98 and Nup214/CAN 104
Nup214/CAN 105
Nup88 105
References 106
7 Import and export at the nuclear envelope 115
Martin Goldberg
Introduction 115
The soluble phase of transport 117
Import of cargo 117
Export of importin |3 118
Recycling of importin a 119
Import and recharging of Ran 120
Role of NPC in transport 120
Translocation and the transporter *- 120
The cytoplasmic filaments 124
The basket 125
Summary 128
References 128
8 Regulating gene expression in mammalian cells: how nuclear architecture
influences mRNA synthesis and export to the cytoplasm 135
Dean A Jackson
Introduction 135
Initiating gene expression 136
• Chromatin structure and gene expression 137
Chromatin modification 138
Spatial nuclear architecture 139
Transcription centres 140
Nuclear architecture and chromosome structure 142
The nuclear matrix 143
Nuclear compartments 144
Proteins of the nuclear matrix - from gene to cytoplasm 145
The nucleoskeleton and nuclear lamina-common themes 146
The lamina genes 147
Lamina function 147
x CONTENTS
Internal nuclear lamins 148
The pathway of gene expression - from gene to cytoplasm 149
RNA export pathways 149
Nuclear transport - facilitated diffusion 150
Gene regulation and transcript stability 150
Conclusions 151
References 152
9 Nuclear shuttling in plant cells 157
Sandra G Lazarowitz, Roisin C McGarry, Yoshimi D Barron and
Miguel E Carvalho
Introduction 157
Nuclear import and export 158
Lessons from animals and yeast 158
Plant cells: The current picture 161
Plant vims movement proteins 165
Geminiviruses encode a nuclear shuttle protein 165
AtNSI, a novel Arabidopsis acetyltransf erase that interacts with NSP 167
A model for AtNSI-NSP interactions ingeminivirus infection 169
Concluding remarks 170
References 172
10 Dynamics of nuclear lamina assembly and disassembly 177
Jos L V Broers and Frans C S Ramaekers
Introduction 177
Lamina dynamics in interphase cells 178
Dynamics of nuclear membrane-associated lamins 178
Dynamics of lamins in intranuclear foci 180
Lamins in nuclear tubules Q 182
Dynamics of nucleoplasmic lamin 183
Lamin dynamics during mitosis 183
Dynamics of the lamina during apoptosis 186
Summary 188
Acknowledgements 188
References 189
11 Spatial and temporal control of nuclear envelope assembly by Ran GTPase 193
Paul R Clarke and Chuanmao Zhang
Introduction 193
Ran GTPase and its regulators 193
Ran determines the direction of nucleocytoplasmic transport 193
Role of Ran in mitotic spindle assembly 194
Control of nuclear envelope assembly by Ran 195
Initial evidence from Xenopus egg extracts 195
Ran induces nuclear envelope formation and nuclear pore complex assembly around
chromatin 196
Interaction of Ran and RCC1 with chromatin 197
Nuclear envelope assembly around Ran beads 197
Roles for importin-f) in nuclear envelope assembly 198
Is the role of Ran in nuclear envelope assembly conserved in all eukaryotes? 200
Summary 201
References 202
CONTENTS xi
12 Nuclear envelope dynamics during mitosis 205
Brian Burke, Melissa Crisp and D avide Salina
Introduction 205
The nuclear envelope 205
Nuclear envelope breakdown 207
Theroleofdynein 208
The kinetochore connection 209
References 213
13 Nuclear dynamics in higher plants 217
David W Galbraith
Introduction 217
What do we know about nuclear structure? 217
A definition of nuclear dynamics 218
How can we measure nuclear dynamics ? 218
The structure of plant nuclei as revealed using GFP targeting 219
Nuclear movement 220
Nuclear fragmentation 221
Dynamic movement of chromosomes and chromatin within the nucleus 221
What mediates the nuclear shape changes? 223
Prospects and future directions 225
Acknowledgements 226
References 226
14 The nuclear envelope in the plant cell cycle 229
David E Evans, Sarah L Irons, Mekdes H Debela and Frederica Bandizzi
Introduction 229
An overview of plant cell division Q 230
A survey of key elements of the endomembrane system involved in the mitotic apparatus 230
Nuclear envelope, endoplasmic reticulum and phragmoplast formation 230
Nuclear pore complexes 232
Traffic of components of the plant NE and of other membranes during cell division 233
LCA1-antigen during mitosis in tomato root cells 233
Mammalian LBR expressed in plants 234
Traffic of other plant NE proteins in cell division 238
Targeting of the plant NE 238
Mechanisms for the breakdown and reformation of the plant NE and for protein traffic during
this process 239
Unanswered questions and future prospects 241
/ References 242
15 Signalling to the nucleus via A-kinase anchoring proteins 245
Philippe Collas, Sandra B Martins and Helga B Landsverk
Summary 245
Introduction 245
Intracellular targeting of cAMP signalling by A-kinase anchoring proteins 246
cAMP signalling via PKA 246
Specifying cAMP signalling by A-kinase anchoring proteins (AKAPs) 246
Regulation of chromosome dynamics and nuclear function by AKAP95 247
xii CONTENTS
Mitotic chromosome condensation in vitro and in somatic cells 247
Involvement of AKAP95 in maternal and paternal chromosome condensation in mouse
zygotes 250
Interphase functions of AKAP95 250
Integration of cAMP and Ca2 + signalling at the cardiomyocyte nuclear envelope by mAKAP 251
Targeting of PP1 to the nuclear envelope by AKAP149: implications on cell cycle progression 252
AKAP149 252
Targeting of PP1 to the nuclear envelope by AKAP149 253
AKAP149 is a B-type lamin-specifying subunit of PP1 254
AKAP149-PP1 association in Gl phase: control of nuclear integrity 255
Anchoring of AMY-1 to S-AKAP84/AKAP149 255
Developmental!/ regulated nAKAP150 255
A novel nuclear envelope-chromatin interaction: involvement in DNA replication 256
Nuclear envelope-chromatin interactions 256
HA95: a protein of the chromatin-nuclear matrix interface 256
Evidence for a roleof the HA95-LAP2 interaction in initiation of DNA replication 257
Conclusions 258
Acknowledgements 258
References 258
16 Spectraplakins and nespins, giant spectrin repeat proteins participating in
the organization of the cytoskeleton and the nuclear envelope 265
Arto Mdd ttd, Christopher J Hutchison and Martin D Watson
Spectraplakins organize actin and microtubule cytoskeletons 265
Spectraplakins harbour actin and microtubule cytoskeletons 266
Calponin-homology domain mediates interactions with actin 267
N-terminal plakin domains can target proteins to cellular junctions but remain poorly
characterized spectraplakins 268
Plectin repeats constitute a specific intermediate filament-binding domain 268
A C-terminal GAS2 domain constitutes a microtubule binding site in spectraplakins 269
Shot and vab-10 mutations underline the importance of spectrplakins in tissue integrity
and morphogenesis 269
The identification of novel spectrin repeat proteins in the nucleus and nuclear membrane 271
Nuclear envelope localization 271
The transmembrane spanning domain is a unique feature of the nesprin family 272
Components of a nucleoskeleton? 272
Influences on cytoplasmic organization 273
Implications for disease 273
Conclusions 273
Reference 274
17 Arabidopsis Ul snRNP 70K protein and its interacting proteins: Nuclear
localization and in vivo dynamics of a novel plant-specific serine/
arginine-rich protein 279
Anireddy S N Reddy, Gul Shad AH and Maxim Golovkin
Introduction 279
U1-70K is essential in plants 281
Arabidopsis U1-70K interacts with a novel set of SR proteins 282
A LAMMER-type protein kinase (AFC2) phosphorylates several plant SR proteins 286
Localization and in vivo dynamics of SR45 288
SR45 is localized to distinct domains in the nucleus 288
CONTENTS xiii
SR45 is highly dynamic in living cells 289
Inhibition of transcription affects intranuclear distribution of GFP-SR45 289
Phosphorylation/dephosphorylation regulate the spatial distribution of GFP-SR45 290
Transcription-dependent redistribution of GFP-SR45 is inhibited by blocking
phosphatase activity of the cell 291
Conclusions 291
Acknowledgements 292
References 292
18 Calcium/calmodulin-binding transcription activators in plants and animals 297
Fawzi Taleb and Hillel Fromm
Calcium: a versatile biological signal 297
Calmodulin as a calcium sensor 298
Regulation of Ca2+/CaM flux by the nuclear envelope 300
CaM-binding proteins 301
Regulation of transcription 303
Transcription factor changes its activity upon ligand binding (from activator to repressor
or the reverse pathway) 303
Ligand binding to transcription factors triggers their movement to their targets 303
Phosphorylation can directly modulate the activity of transcription factors on at least
five levels of regulation 303
CaM-regulated transcription factors 305
DNA-binding specificity of CAMTAs 306
The physiological role of CAMTA under stress conditions 308
Future perspectives 311
References 312
19 CAAX-dependent modifications of the lamin proteins in the organization
of the nuclear periphery ^ 317
C P Maske and D J Vaux
Introduction 317
The biochemistry of lamin CAAX processing 318
Biological consequences of CAAX processing of the nuclear lamins 321
Defects of lamin CAAX processing: drugs and diseases 323
Conclusions 325
References 325
20 All in the family: evidence for four new LEM-domain proteins Lem2
(NET-25), Lem3, Lem4 and Lem5 in the human genome 329
Kenneth K Lee and Katherine L Wilson
Summary 329
Introduction to LEM-domain proteins, their functions in the nucleus and links to
laminopathy disease 329
Evidence for more LEM-domain proteins in the human genome 332
Other new LEM-domain proteins? 335
Acknowledgements 335
References 335
Index 340
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spelling | The nuclear envelope edited by D.E. Evans ... Abingdon, Oxon, OX, UK BIOS Scientific Publishers 2004 xviii, 344 p. ill. (some col.) 24 cm txt rdacontent n rdamedia nc rdacarrier Includes bibliographical references and index Membranes nucléaires aNuclear membranes Kernhülle (DE-588)4309987-7 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Kernhülle (DE-588)4309987-7 s b DE-604 Evans, David E. Sonstige oth http://www.loc.gov/catdir/toc/ecip0417/2004009192.html Table of contents HEBIS Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=012997350&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
spellingShingle | The nuclear envelope Membranes nucléaires aNuclear membranes Kernhülle (DE-588)4309987-7 gnd |
subject_GND | (DE-588)4309987-7 (DE-588)4143413-4 |
title | The nuclear envelope |
title_auth | The nuclear envelope |
title_exact_search | The nuclear envelope |
title_full | The nuclear envelope edited by D.E. Evans ... |
title_fullStr | The nuclear envelope edited by D.E. Evans ... |
title_full_unstemmed | The nuclear envelope edited by D.E. Evans ... |
title_short | The nuclear envelope |
title_sort | the nuclear envelope |
topic | Membranes nucléaires aNuclear membranes Kernhülle (DE-588)4309987-7 gnd |
topic_facet | Membranes nucléaires aNuclear membranes Kernhülle Aufsatzsammlung |
url | http://www.loc.gov/catdir/toc/ecip0417/2004009192.html http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=012997350&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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