E-Book, Englisch, 331 Seiten
Liu The Plant Cytoskeleton
1. Auflage 2010
ISBN: 978-1-4419-0987-9
Verlag: Springer-Verlag
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)
E-Book, Englisch, 331 Seiten
ISBN: 978-1-4419-0987-9
Verlag: Springer-Verlag
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)
Autoren/Hrsg.
Weitere Infos & Material
1;Preface;6
2;Contents;8
3;Contributors;10
4;Part I Molecular Basis of the Plant Cytoskeleton;14
4.1;Chapter 1: Actin Functions in the Cytoplasmic and Nuclear Compartments;15
4.1.1;1.1 Introduction;15
4.1.2;1.2 Evolutionary Origin and Phylogeny of Plant Actins and Actin Binding Proteins;16
4.1.3;1.3 The Actin Cytoskeleton in Plant Cell Polarity and Elongation;19
4.1.3.1;1.3.1 Genetic Studies Demonstrate the Role of Actin and ABP Variants in Cell Polarity and Elongation;19
4.1.3.2;1.3.2 F-Actin Filament Dynamics and Cell Elongation;22
4.1.3.3;1.3.3 Protein Variant Differences vs. Gene Regulation;25
4.1.3.4;1.3.4 Protein–Protein Interactions Among Actin and ABP Families;28
4.1.3.5;1.3.5 Organelle Streaming and Vesicle Movement Within a Relatively Stationary Cytoplasm;29
4.1.4;1.4 Nuclear Actin;31
4.1.4.1;1.4.1 History of Nuclear Actin Research;31
4.1.4.2;1.4.2 Plant Actin and ABPs in the Nucleus;31
4.1.4.3;1.4.3 Molecular Genetic Functions of Nuclear Actin;33
4.1.4.4;1.4.4 Epigenetic Functions for Actin in the Assembly of Chromatin Remodeling and Modifying Complexes;33
4.1.5;1.5 Actins and ADFs in Signal Transduction;35
4.1.6;References;37
4.2;Chapter 2: Plant Myosins;45
4.2.1;2.1 Introduction;45
4.2.2;2.2 Domain Structures of Plant Myosin Heavy Chains;47
4.2.3;2.3 The Motor Domain;48
4.2.4;2.4 The Directional Determinant of Organelle Transport by the Polarity of Acitn Filaments;49
4.2.5;2.5 The Neck Domain;50
4.2.6;2.6 a-Helical Coiled-Coil Domain in the Tail Region;51
4.2.7;2.7 Processive Movement of Higher Pant Myosin XI;53
4.2.8;2.8 Regulation of Higher Plant Myosin XI Through CaM Light Chain;54
4.2.9;2.9 Regulation of Cytoplasmic Streaming or Organelle Transports in Pollen Tubes;55
4.2.10;2.10 Globular Tail Domain;55
4.2.11;2.11 The Mechanism for Cargo Recognition by Higher Plant Myosin XI;56
4.2.12;2.12 Functional Inter-Domain Communication Between a-Helical Coiled-Coil and Globular Tail Domains;58
4.2.13;2.13 Direct Binding of Chara Myosin XI to Phospholipid Vesicles;59
4.2.14;2.14 Cytoplasmic Streaming in Characean Cells;59
4.2.15;2.15 The Regulation of Cytoplasmic Streaming in the Characean Cell;60
4.2.16;2.16 Cytoplasmic Streaming in Higher Plant Cells;61
4.2.17;2.17 Conclusion;62
4.2.18;References;63
4.3;Chapter 3: Actin-Binding Proteins and Actin Dynamics in Plant Cells;69
4.3.1;3.1 Introduction;70
4.3.2;3.2 Profilin;71
4.3.3;3.3 Arp2/3 Complex and Its Regulatory WAVE Complex;73
4.3.4;3.4 Formin;75
4.3.5;3.5 Capping Protein (CP);77
4.3.6;3.6 Actin Depolymerizing Factors (ADFs);78
4.3.7;3.7 Villin/Gelsolin/Fragmin Superfamily Proteins;80
4.3.8;3.8 Conclusions;83
4.3.9;References;84
4.4;Chapter 4: Microtubule Nucleation and Organization in Plant Cells;93
4.4.1;4.1 Introduction;93
4.4.2;4.2 Microtubule Nucleation Sites in Land Plant Cells;93
4.4.2.1;4.2.1 Patterns of Microtubules in the Cell Cycle of Land Plants;93
4.4.2.2;4.2.2 Microtubule Nucleation in Interphase Cells;95
4.4.2.2.1;4.2.2.1 Nucleation Sites for the Cortical Array;95
4.4.2.2.2;4.2.2.2 Nucleation Sites for the Radial Array;96
4.4.2.3;4.2.3 Microtubule Nucleation for Preprophase Band Development;96
4.4.2.4;4.2.4 Microtubule Nucleation in Mitosis;97
4.4.2.4.1;4.2.4.1 Three Pathways in Metazoan Cells;97
4.4.2.4.2;4.2.4.2 Origin of Spindle Microtubules at Prophase;98
4.4.2.4.3;4.2.4.3 Microtubule Nucleation Sites During Spindle Development;98
4.4.2.5;4.2.5 Microtubule Nucleation in Cytokinesis;99
4.4.3;4.3 Proteins Involved in Microtubule Nucleation;99
4.4.3.1;4.3.1 g-Tubulin Complexes;99
4.4.3.2;4.3.2 Other Centrosomal Proteins;100
4.4.3.3;4.3.3 Is There g-Tubulin-Independent Nucleation?;101
4.4.4;4.4 Role of Microtubule Nucleation in Microtubule Organization;101
4.4.5;4.5 Concluding Remarks;102
4.4.6;References;103
4.5;Chapter 5: Microtubule Plus End-Tracking Proteins and Their Activities in Plants;107
4.5.1;5.1 Introduction;107
4.5.2;5.2 Microtubule Structure and Dynamics;109
4.5.3;5.3 Holding onto a Moving Target: How +TIPs Find, Recognize and Maintain Contact with the Plus End;110
4.5.4;5.4 +TIPs and Their Role in the Cell;112
4.5.5;5.5 +TIPs in Plants;112
4.5.6;5.6 EB1, the Quintessential +TIP;114
4.5.7;5.7 Structural Conservation Amongst EB1 Family Members;114
4.5.8;5.8 EB1 Localization Patterns in Plant Cells;115
4.5.9;5.9 EB1 and the Regulation of Microtubule Dynamics;116
4.5.10;5.10 EB1 and +TIP Complex Assembly;117
4.5.11;5.11 Proteins Bearing TOG Domains: MOR1 and CLASP;118
4.5.12;5.12 Plant Kinesins and ATK5;119
4.5.13;5.13 Actin-Related Proteins;121
4.5.14;5.14 Plant-Specific +TIPs;121
4.5.15;5.15 Conclusions and Unanswered Questions;122
4.5.16;References;123
4.6;Chapter 6: Microtubule Motor Proteins in the Eukaryotic Green Lineage: Functions and Regulation;130
4.6.1;6.1 Introduction;130
4.6.2;6.2 Kinesins;131
4.6.3;6.3 Kinesin Types and Evolutionary Relationships;131
4.6.4;6.4 Domains in Kinesins;138
4.6.5;6.5 Known Functions of Kinesins in Plants;140
4.6.6;6.6 Structure and Regulation of Kinesins;145
4.6.7;6.7 Concluding Remarks;148
4.6.8;References;148
5;Part II Cytoskeletal Reorganization in Plant Cell Division;153
5.1;Chapter 7: The Preprophase Band and Division Site Determination in Land Plants;154
5.1.1;7.1 Introduction;154
5.1.1.1;7.1.1 Focus of this Chapter;154
5.1.1.2;7.1.2 What is a PPB?;155
5.1.1.3;7.1.3 To Have or Not to Have a PPB;156
5.1.1.4;7.1.4 The PPB in Evolution;156
5.1.2;7.2 The PPB and the Cell Cycle;157
5.1.2.1;7.2.1 A Coupling Between Cell Cycle and PPB Formation?;157
5.1.2.2;7.2.2 The Cell Cycle and G2/M Transition;157
5.1.2.2.1;7.2.2.1 Cyclin-Dependent Kinases;160
5.1.2.2.2;7.2.2.2 Cyclins;160
5.1.2.2.3;7.2.2.3 CDK Inhibitors;160
5.1.2.2.4;7.2.2.4 CKS Proteins;161
5.1.2.2.5;7.2.2.5 Regulation of CDK Complexes by Phosphorylation;161
5.1.2.3;7.2.3 Core Cell Cycle Proteins Identified at the PPB;161
5.1.3;7.3 The PPB and the Pre-Mitotic Cell;163
5.1.3.1;7.3.1 The Nucleus;163
5.1.3.2;7.3.2 Vacuoles and the Phragmosome;164
5.1.3.3;7.3.3 Golgi Apparatus and Endocytosis;165
5.1.4;7.4 Structure and Dynamics of the PPB;165
5.1.4.1;7.4.1 Microtubules;165
5.1.4.1.1;7.4.1.1 MT Dynamics at the Cortex;166
5.1.4.1.2;7.4.1.2 Origin and Dynamics of PPB Microtubules;166
5.1.4.1.3;7.4.1.3 Non PPB Microtubules During the G2/M Transition;167
5.1.4.2;7.4.2 Actin;169
5.1.4.3;7.4.3 Proteins Localized to the PPB: A Critical Review;170
5.1.4.3.1;7.4.3.1 Preliminary Remarks;170
5.1.4.3.2;7.4.3.2 Proteins Potentially Involved in PPB Formation;170
5.1.4.3.3;7.4.3.3 Proteins Potentially Involved in CDS Establishment;178
5.1.5;7.5 The PPB and the Division Plane of Plant Cells;179
5.1.5.1;7.5.1 Introduction;179
5.1.5.2;7.5.2 Mutations Affecting the PPB;179
5.1.5.3;7.5.3 The PPB and Cortical Division Site Establishment;183
5.1.5.4;7.5.4 The PPB and the Prophase Spindle;184
5.1.6;7.6 Conclusions;185
5.1.7;References;186
5.2;Chapter 8: Acentrosomal Spindle Formation Through the Heroic Age of Microscopy: Past Techniques, Present Thoughts, and Future Directions;195
5.2.1;8.1 Early Fixation Techniques;196
5.2.2;8.2 Light Microscopy Techniques;198
5.2.3;8.3 Transmission Electron Microscopy (TEM) Techniques;200
5.2.4;8.4 Fluorescence Microscopy: Immunofluorescence;202
5.2.5;8.5 Fluorescent Microscopy Techniques: Intrinsic Fluorescent Proteins;205
5.2.6;8.6 Acentrosomal Bipolarity Organized by the PPB;208
5.2.7;8.7 The Future Directions in Acentrosomal Spindle Formation;209
5.2.8;References;210
5.3;Chapter 9: Microtubule Organization in the Phragmoplast;214
5.3.1;9.1 Introduction;214
5.3.2;9.2 Microtubule-Interacting Factors in the Phragmoplast;216
5.3.3;9.3 Organization of Microtubule Minus Ends in the Phragmoplast;221
5.3.4;9.4 Organization of Microtubule Plus Ends in the Phragmoplast;222
5.3.5;9.5 Stability and Turnovers of Microtubules in the Phragmoplast;223
5.3.6;9.6 Regulation of Phragmoplast MT Dynamics by Post-Translational Modifications;224
5.3.7;9.7 Conclusion: Assembly of the Phragmoplast by Mini-Phragmoplasts;225
5.3.8;References;226
6;Part III The Cytoskeleton in Plant Growth and Development;233
6.1;Chapter 10: Signaling to the Cytoskeleton in Diffuse Cell Growth;234
6.1.1;10.1 Signals Modulating Diffuse Cell Growth;235
6.1.1.1;10.1.1 Phytohormones;235
6.1.1.2;10.1.2 Mechanical Signals;237
6.1.2;10.2 Signal Transduction Pathways Regulating MFs;238
6.1.3;10.3 Signal Transduction Pathways that Transmit Signals to MTs;240
6.1.3.1;10.3.1 ROP GTPase Signaling;241
6.1.3.2;10.3.2 Protein Kinases and Phosphatases;242
6.1.3.2.1;10.3.2.1 Perspective;242
6.1.4;References;243
6.2;Chapter 11: Microtubule and Cell Shape Determination;249
6.2.1;11.1 Microtubules Determine Cell Shape;249
6.2.2;11.2 Distinct MT Array Organization Correlates with Cell Shape: Wild-Type Cells;250
6.2.3;11.3 Helical Growth as an Unusual Case of Growth Anisotropy;251
6.2.4;11.4 Helical MT Organization Underlies Skewed Cell Growth;254
6.2.5;11.5 Toward Elucidation of Symmetry-Breaking Factors;256
6.2.6;11.6 Tissue Morphology Affects Microtubule Alignment;258
6.2.7;References;259
6.3;Chapter 12: Cytoskeleton and Root Hair Growth;262
6.3.1;12.1 Introduction;262
6.3.2;12.2 Root Hair Initiation;263
6.3.2.1;12.2.1 Selection of the Bulge Site;263
6.3.2.2;12.2.2 The Cytoskeleton in Bulge Formation;264
6.3.3;12.3 Root Hair Tip Growth: General Considerations and Organelle Distribution;265
6.3.3.1;12.3.1 Actin Cytoskeleton in Root Hair Tip Growth;265
6.3.3.2;12.3.2 Myosin in Root Hair Tip Growth;267
6.3.3.3;12.3.3 Microtubules and Root Hair Tip Growth;268
6.3.3.4;12.3.4 Membrane Trafficking and Tip Growth;269
6.3.3.5;12.3.5 Signaling Factors in Tip Growth;271
6.3.4;12.4 Conclusions;272
6.3.5;References;274
6.4;Chapter 13: Microtubules, MAPs and Xylem Formation;279
6.4.1;13.1 Introduction;279
6.4.2;13.2 Microtubule Organization in Xylem Cells;282
6.4.3;13.3 Impact of Pharmacological Treatments on Microtubules in Xylem Cells;288
6.4.4;13.4 Reorientation of the Microtubule Network Axis During Xylem Cell Formation;291
6.4.5;13.5 Expression of Microtubule and MAP Genes During Xylem Formation;292
6.4.5.1;13.5.1 Tubulin During Xylem Formation;292
6.4.5.2;13.5.2 MAP70 Microtubule Associated Protein During Xylem Vessel Formation;293
6.4.5.3;13.5.3 MIDD1 Microtubule Plus-End Associated Protein During Xylem Vessel Formation;294
6.4.5.4;13.5.4 The Cross-Bridging MAP65 During Xylem Vessel Formation;296
6.4.5.5;13.5.5 FRA1 Kinesin During Xylem Cell Wall Formation;297
6.4.5.6;13.5.6 FRA2 Katanin During Xylem Cell Wall Formation;299
6.4.5.7;13.5.7 MAP20s During Xylem Cell Wall Formation;299
6.4.6;13.6 Microtubules and Cellulose Synthesis in Xylem Cells;299
6.4.7;13.7 Microtubules and the Global Patterning of the Xylem Cell Wall;300
6.4.8;13.8 Conclusion;302
6.4.9;References;303
6.5;Chapter 14: The Cytoskeleton and Root Growth Behavior;309
6.5.1;14.1 Introduction;309
6.5.2;14.2 Roots Grow Using a Combination of Cell Division and Cell Expansion;312
6.5.2.1;14.2.1 Controlled Cell Division Contributes to Root Growth;312
6.5.2.2;14.2.2 Regulated Cell Expansion Also Contributes to Root Growth;313
6.5.3;14.3 Mutations in Tubulin Genes Affect Microtubule Arrays and Root Skewing;314
6.5.4;14.4 Mutations in Microtubule Associated Proteins Also Lead to Abnormal Root Development;315
6.5.5;14.5 Other Mutations that Alter Root Growth Behavior;319
6.5.6;14.6 Natural Variation in Root Growth Behavior;322
6.5.7;14.7 Closing Remarks;324
6.5.8;References;324
7;Index;329




