Peer / Schulz The Plant Plasma Membrane

1. Auflage 2010
ISBN: 978-3-642-13431-9
Verlag: Springer
Format: PDF
Kopierschutz: Adobe DRM (»Systemvoraussetzungen)

E-Book, Englisch, 494 Seiten

In plant cells, the plasma membrane is a highly elaborated structure that functions as the point of exchange with adjoining cells, cell walls and the external environment. Transactions at the plasma membrane include uptake of water and essential mineral nutrients, gas exchange, movement of metabolites, transport and perception of signaling molecules, and initial responses to external biota. Selective transporters control the rates and direction of small molecule movement across the membrane barrier and manipulate the turgor that maintains plant form and drives plant cell expansion. The plasma membrane provides an environment in which molecular and macromolecular interactions are enhanced by the clustering of proteins in oligimeric complexes for more efficient retention of biosynthetic intermediates, and by the anchoring of protein complexes to promote regulatory interactions. The coupling of signal perception at the membrane surface with intracellular second messengers also involves transduction across the plasma membrane. Finally, the generation and ordering of the external cell walls involves processes mediated at the plant cell surface by the plasma membrane. This volume is divided into three sections. The first section describes the basic mechanisms that regulate all plasma membrane functions. The second describes plasma membrane transport activity. The final section of the book describes signaling interactions at the plasma membrane. These topics are given a unique treatment in this volume, as the discussions are restricted to the plasma membrane itself as much as possible. A more complete knowledge of the plasma membrane’s structure and function is essential to current efforts to increase the sustainability of agricultural production of food, fiber, and fuel crops.

Autoren/Hrsg.

Peer, Wendy

Schulz, Burkhard

Inhaltsverzeichnis

1;Editors;6
2;Preface;8
3;Contents;12
4;Section I Plasma Membrane Structure and Basic Functions;16
4.1;Lipids of the Plant Plasma Membrane;17
4.1.1;1 Biochemical Analysis of Plant Plasma Membrane;18
4.1.1.1;1.1 Isolation of Highly Purified Plasma Membrane Fractions from Plant Tissues;18
4.1.1.2;1.2 Lipid Content of Plant Plasma Membrane;18
4.1.1.2.1;1.2.1 Glycerolipids;20
4.1.1.2.1.1;Structural Glycerolipids;22
4.1.1.2.1.2;Phosphoinositides;24
4.1.1.2.1.3;PI(3)P and PI 3-Kinase;24
4.1.1.2.1.4;PI(4)P and PI 4-Kinase;26
4.1.1.2.1.5;PI(5)P;27
4.1.1.2.1.6;PI(4,5)P2 and PIP Kinase;27
4.1.1.2.1.7;Phosphatidic Acid/Diacylglycerol Pyrophosphate;27
4.1.1.2.2;1.2.2 Sphingolipids;27
4.1.1.2.3;1.2.3 Plant Sterols;29
4.1.1.3;1.3 Asymmetrical Distribution of Lipids Across the Plasma Membrane;32
4.1.2;2 Evidence for Membrane Domains in the Plant Plasma Membrane;33
4.1.2.1;2.1 Organization of Lipids Within the Plasma Membrane: The Concept of Membrane Rafts;33
4.1.2.2;2.2 Characterization of Detergent-Insoluble Plasma Membranes from Plants;35
4.1.2.2.1;2.2.1 Sterols;35
4.1.2.2.2;2.2.2 Sphingolipids;36
4.1.2.2.3;2.2.3 Phospholipids;36
4.1.2.2.4;2.2.4 Protein Content;37
4.1.2.3;2.3 Visualization of Rafts in Plant Plasma Membrane;38
4.1.2.4;2.4 Putative Roles of Plasma Membrane Raft in Plant Biology;38
4.1.3;3 Conclusions;40
4.1.4;References;40
4.2;Plasma Membrane Protein Trafficking;45
4.2.1;1 Types of Trafficking at the Plasma Membrane;45
4.2.2;2 Exocytosis/Secretion/Anterograde Trafficking;47
4.2.2.1;2.1 Clathrin-Coated Vesicles;48
4.2.2.2;2.2 Adaptins and Adaptor Protein Complexes;49
4.2.2.3;2.3 Vesicle Fusion with the Plasma Membrane;50
4.2.2.4;2.4 Exocyst;52
4.2.2.5;2.5 Secretory Vesicle Cluster;52
4.2.2.6;2.6 The Microtubule-Associated Cellulose Synthase Compartment;53
4.2.3;3 Endocytosis/Retrograde Trafficking;53
4.2.3.1;3.1 Clathrin-Mediated Endocytosis;54
4.2.3.2;3.2 Receptor-Mediated Endocytosis;55
4.2.3.3;3.3 Sorting and the Return Trip to the PM;57
4.2.3.4;3.4 Endosomes and Multivesicular Bodies;58
4.2.4;4 Role of the Cytoskeleton in Plasma Membrane Protein Trafficking;59
4.2.4.1;4.1 Actin;59
4.2.4.2;4.2 Microtubules;60
4.2.5;5 Models of Trafficking;60
4.2.5.1;5.1 Constitutive;62
4.2.5.2;5.2 Induced;62
4.2.5.3;5.3 Specialized;63
4.2.6;6 Concluding Remarks;64
4.2.7;References;64
4.3;The Plasma Membrane and the Cell Wall;71
4.3.1;1 Introduction;71
4.3.2;2 Primary and Secondary Cell Walls;72
4.3.2.1;2.1 Primary Cell Walls;74
4.3.2.2;2.2 Secondary Cell Walls;75
4.3.3;3 Golgi-Associated Cell Wall Metabolism;76
4.3.4;4 Apoplastic Components and Processes;78
4.3.4.1;4.1 Expansins and Glycosyl Hydrolases;78
4.3.4.2;4.2 Nonenzymatic Apoplastic Proteins;79
4.3.4.3;4.3 Glycosylphosphatidylinositol Anchors;80
4.3.5;5 Callose;81
4.3.6;6 Cellulose;82
4.3.6.1;6.1 The Cellulose Synthase A Complex;82
4.3.6.2;6.2 Structural Organization of the CESA Proteins;83
4.3.6.3;6.3 Cellulose Synthesis;84
4.3.6.4;6.4 Mutational Analyses of Cell Wall Formation;84
4.3.6.4.1;6.4.1 Mutations Affecting Cellulose Formation in the Primary Cell Wall;84
4.3.6.4.2;6.4.2 Mutations Affecting Secondary Cell Wall Cellulose;86
4.3.6.5;6.5 Inhibitory Drugs;87
4.3.7;7 Cell Wall Signaling;87
4.3.7.1;7.1 Receptor-Like Kinases;88
4.3.7.2;7.2 Wall-Associated Kinases;88
4.3.8;8 Outlook;90
4.3.9;References;90
4.4;Plasmodesmata and Non-Cell-Autonomous Signaling in Plants;100
4.4.1;1 Introduction;101
4.4.2;2 Plasmodesmata Are Membrane-Lined Cytoplasmic Channels;102
4.4.3;3 Formation of Plasmodesmata;104
4.4.3.1;3.1 Primary Plasmodesmata;104
4.4.3.2;3.2 Secondary and Modified Plasmodesmata;104
4.4.4;4 Plasmodesmata in Lower Plants;106
4.4.4.1;4.1 Brown Algae: Laminaria;107
4.4.4.2;4.2 Green Algae: Chara;107
4.4.4.3;4.3 Bryophytes;108
4.4.5;5 Proteins Localized at or Near Plasmodesmata;108
4.4.6;6 PD Mediate Macromolecular Trafficking;109
4.4.6.1;6.1 KN1 Moves Through Plasmodesmata to Act Non-Cell-Autonomously;110
4.4.6.2;6.2 CPC and SHR ;111
4.4.6.3;6.3 Mechanism of PD Trafficking;113
4.4.7;7 Tunneling Nanotubes: Animal Analog of Plasmodesmata?;114
4.4.8;8 Concluding Remarks;115
4.4.9;References;116
4.5;Posttranslational Modifications of Plasma Membrane Proteins and Their Implications for Plant Growth and Development;121
4.5.1;1 Control of Protein Targeting via Covalent Protein Modifications;121
4.5.1.1;1.1 Myristoylation;122
4.5.1.2;1.2 Prenylation;122
4.5.1.3;1.3 S-Acylation;124
4.5.1.4;1.4 Lipid Modification Targets;125
4.5.1.5;1.5 GPI Anchors;127
4.5.1.6;1.6 GPI-Anchored Proteins;129
4.5.1.7;1.7 Phosphorylation as a Determinant for Membrane Protein Targeting;132
4.5.2;2 Concluding Remarks;134
4.5.3;References;134
5;Section II Plasma Membrane Transporters;141
5.1;Functional Classification of Plant Plasma Membrane Transporters;142
5.1.1;1 Introduction into Plasma Membrane Transport;142
5.1.2;2 Types of Membrane Transport;143
5.1.2.1;2.1 Passive Transport;143
5.1.2.2;2.2 Active Transport;145
5.1.3;3 Passive Transport Through the PM;145
5.1.3.1;3.1 Channels;146
5.1.3.1.1;3.1.1 Anion Channels;146
5.1.3.1.2;3.1.2 Aluminum-Activated Malate Transporters;147
5.1.3.1.3;3.1.3 Slow Anion Channel-Associated 1;147
5.1.4;4 Cation Channels;148
5.1.4.1;4.1 K+ Channels;148
5.1.4.1.1;4.1.1 Shaker-Type K+ Channels;148
5.1.4.1.1.1;Inward-Rectifying Shaker-Type Channels;148
5.1.4.1.1.2;Outward-Rectifying Channels;149
5.1.4.1.1.3;Tandem Pore K+ Channel;150
5.1.4.1.1.4;High-Affinity K+ Transporters;150
5.1.4.1.1.5;KUP/HAK/KT Permeases;151
5.1.5;5 Ca2+ Channels;151
5.1.5.1;5.1 Cyclic Nucleotide-Gated Channels;152
5.1.5.2;5.2 GluR (Ionotropic Glutamate Receptor Channel Homologs);152
5.1.5.3;5.3 Annexins and Ca2+ Transport;152
5.1.5.4;5.4 Voltage-Dependent and Mechanosensitive Ca2+ Channels;153
5.1.6;6 Pumps;153
5.1.6.1;6.1 P-Type ATPases;153
5.1.6.1.1;6.1.1 P3A-Type H+-ATPase;153
5.1.6.1.2;6.1.2 P2B-(Ca2+) ATPase;154
5.1.6.1.3;6.1.3 P1B-Zn2+-ATPase;154
5.1.6.2;6.2 H+-Pyrophosphorylase;154
5.1.6.3;6.3 ABC Transporters;155
5.1.6.3.1;6.3.1 Phytohormone Transport and ABC Transporters;156
5.1.7;7 The PIN-FORMED (PIN) Transporter Family;157
5.1.8;8 Amino Acid/Auxin Permease Transporters;158
5.1.8.1;8.1 Amino Acid-Polyamine-Choline Transporters;158
5.1.8.2;8.2 Amino Acid Transporter Family;158
5.1.8.2.1;8.2.1 Amino Acid Permeases;159
5.1.8.2.2;8.2.2 AAAP Transporters Involved in Auxin Transport;159
5.1.8.2.3;8.2.3 Lysine/Histidine Transporters;160
5.1.8.2.4;8.2.4 Proline Transporters;160
5.1.8.2.5;8.2.5 GABA Transporters;160
5.1.8.2.6;8.2.6 Aromatic and Neutral Amino Acid Transporters;161
5.1.8.3;8.3 Peptide Transporters;161
5.1.8.3.1;8.3.1 PTR/NRT1 Peptide Transporters;161
5.1.8.3.2;8.3.2 Oligopeptide Transporter;162
5.1.8.4;8.4 Ammonium Transporters;162
5.1.9;9 Sugar Transporters;163
5.1.9.1;9.1 Monosaccharide Transporters;163
5.1.9.1.1;9.1.1 Sugar Transport Protein;164
5.1.9.1.2;9.1.2 Inositol Transporter;164
5.1.9.1.3;9.1.3 Polyol Transporter;164
5.1.9.2;9.2 Sucrose Transporter;164
5.1.10;10 Purine Permease;165
5.1.11;11 Aquaporins;166
5.1.12;12 Nitrate Transporter;168
5.1.13;13 Sulfate Transporter;169
5.1.13.1;13.1 SulP Gene Family;169
5.1.14;14 Metal Transporter;170
5.1.14.1;14.1 Iron Transporter;170
5.1.14.1.1;14.1.1 ZIP Transporters;171
5.1.14.1.2;14.1.2 Natural Resistance-Associated Macrophage Protein;171
5.1.14.1.3;14.1.3 Copper Transporter;172
5.1.14.1.4;14.1.4 SLC40 Transporters;172
5.1.14.2;14.2 Chelation-Based Strategy of Iron Uptake;172
5.1.14.2.1;14.2.1 Yellow Stripe1-Like Transporter;173
5.1.15;15 Phosphate Transporter;173
5.1.16;16 Conclusion;174
5.1.17;References;174
5.2;Plasma Membrane ATPases;188
5.2.1;1 Introduction;188
5.2.2;2 Plasma Membrane H+-ATPases (P3-ATPases);190
5.2.3;3 Regulation of PM P-Type H+-ATPases;193
5.2.4;4 Plasma Membrane Ca2+-ATPases (P2B-ATPases);195
5.2.5;5 Plasma Membrane Zn2+-ATPases (P1B-ATPases);196
5.2.6;6 Additional Plasma Membrane P-Type ATPases;197
5.2.7;References;198
5.3;Physiological Roles for the PIP Family of Plant Aquaporins;204
5.3.1;1 Introduction;204
5.3.2;2 Aquaporin Substrates;206
5.3.2.1;2.1 PIPs: Mostly Water Channels and Mostly on the PM and Trafficking Vesicles;207
5.3.2.2;2.2 Regulation of PIP AQP Expression and Activity;208
5.3.2.2.1;2.2.1 Phosphorylation;209
5.3.2.2.2;2.2.2 Quaternary Structure;210
5.3.2.2.3;2.2.3 Regulation by the Cellular Environment;210
5.3.3;3 Subcellular Distribution and Protein Trafficking;211
5.3.4;4 Multiple Physiological Roles for PIP Aquaporins;212
5.3.4.1;4.1 The Role of PIPs in Seed Germination;218
5.3.4.2;4.2 PIPs in Elongation Growth and Differentiation;219
5.3.4.3;4.3 A Role for PIPs in Programmed Cell Death and Plant Microbe Interactions;220
5.3.4.4;4.4 Roles of PIPs in Adaptation to Environmental Challenges;222
5.3.5;5 Perspectives;225
5.3.6;References;226
5.4;The Role of Plasma Membrane Nitrogen Transporters in Nitrogen Acquisition and Utilization;234
5.4.1;1 Introduction;234
5.4.2;2 Nitrate Transporters;235
5.4.2.1;2.1 Nitrate Uptake;236
5.4.2.2;2.2 Nitrate Xylem Loading;238
5.4.2.3;2.3 Nitrate Remobilization;239
5.4.2.4;2.4 Nitrate and Embryo Development;239
5.4.3;3 Ammonium Transporters;239
5.4.3.1;3.1 Ammonium Uptake;240
5.4.3.2;3.2 AtAMT2.1 and AtAMT1.4;241
5.4.4;4 Amino Acid Transporters;241
5.4.4.1;4.1 Amino Acid Uptake;242
5.4.4.2;4.2 Long Distance Transport of Amino Acids;243
5.4.4.3;4.3 Amino Acid Transport and the Embryo;243
5.4.5;5 Conclusions;244
5.4.6;References;244
5.5;Plant Plasma Membrane and Phosphate Deprivation;248
5.5.1;1 Introduction;248
5.5.2;2 Plasma Membrane Components Modulated by Phosphate Availability;249
5.5.2.1;2.1 Glycerolipids;249
5.5.2.1.1;2.1.1 Lipid Composition of Plasma Membrane;249
5.5.2.1.2;2.1.2 Phosphate Deprivation Promotes Phospholipid Recycling and Digalactolipid Accumulation in Plasma Membrane;250
5.5.3;3 Transporters;252
5.5.3.1;3.1 Phosphate Transporters;252
5.5.3.2;3.2 Metal Transporters;254
5.5.4;4 Timing and Regulation of Phosphate Deficiency-Related Modifications Affecting the Plasma Membrane;255
5.5.5;5 Conclusion;258
5.5.6;References;258
5.6;Biology of Plant Potassium Channels;263
5.6.1;1 Introduction;263
5.6.2;2 Milestones in Plant Potassium Channel Research;265
5.6.3;3 Stomatal Movement Is Based on the Reversible Expansion of Guard Cell Pairs;271
5.6.4;4 Growth Results from Irreversible Cell Expansion;273
5.6.5;5 Polar Growth is Best Studied in Root Hairs and Pollen Tubes;274
5.6.5.1;5.1 Root Hairs;274
5.6.5.2;5.2 Pollen Tubes;275
5.6.6;6 Long Distance K+ Transport in Plants;276
5.6.7;7 Potassium Channels Control Cell Cycle Progression;276
5.6.8;8 Vacuolar K+ Channels;277
5.6.9;9 Outlook;278
5.6.10;References;278
5.7;Mechanism and Evolution of Calcium Transport Across the Plant Plasma Membrane;285
5.7.1;1 Introduction;285
5.7.2;2 PM Ca2+ Transport Pathways;286
5.7.2.1;2.1 Ca2+ Influx Channels;287
5.7.2.1.1;2.1.1 Ca2+ Influx by Nonselective Cation Channels;287
5.7.2.1.2;2.1.2 Gene Candidates for Plant PM Ca2+-Permeable Channels;288
5.7.2.2;2.2 Ca2+ Efflux Transporters;289
5.7.2.2.1;2.2.1 Ca2+-ATPases;289
5.7.2.2.2;2.2.2 Ca2+/H+ ExchangersCa2+/H+ exchangers (CAX);291
5.7.3;3 Evolution of PM Ca2+ Transporters in Plants;291
5.7.3.1;3.1 PM Ca2+ Transport in Lower Plants;291
5.7.3.2;3.2 Analysis of PM Ca2+ Transport by Comparative Genomics;293
5.7.4;4 Conclusions;295
5.7.5;References;295
5.8;Sulfate Transport;300
5.8.1;1 Introduction;300
5.8.1.1;1.1 Physiology and Energetics of Sulfate Uptake in Plants;301
5.8.1.2;1.2 Efflux Across the Plasma Membrane;302
5.8.2;2 The SulP Gene Family;302
5.8.2.1;2.1 Structure of the Sulfate Transporters;305
5.8.2.2;2.2 Mechanisms of Regulation;306
5.8.3;3 Perspective;307
5.8.4;References;307
5.9;Metal Transport;311
5.9.1;1 Introduction;311
5.9.2;2 Iron;312
5.9.2.1;2.1 Chelation Strategy for Iron Uptake;313
5.9.2.1.1;2.1.1 Yellow Stripe and Yellow Stripe-Like Transporters;313
5.9.2.2;2.2 Reduction Strategy for Iron Uptake;316
5.9.3;3 ZIP Family of Metal Transporters;317
5.9.3.1;3.1 Structure and Function of ZIP Transporters;318
5.9.3.2;3.2 ZIP Transporters in Plants;318
5.9.4;4 NRAMP Family of Metal Transporters;320
5.9.4.1;4.1 P1B-ATPase Family of Metal Transporters;322
5.9.5;5 COPT Family of Metal Transporters;325
5.9.6;6 CDF Family of Metal Transporters;326
5.9.7;7 SLC40 Family of Metal Transporters;327
5.9.8;8 Cation Selectivity;328
5.9.9;9 Conclusion;330
5.9.10;References;330
5.10;Organic Carbon and Nitrogen Transporters;339
5.10.1;1 Introduction;339
5.10.2;2 Organic Nitrogen Transporters;341
5.10.2.1;2.1 Amino Acid Transporters;341
5.10.2.1.1;2.1.1 Amino Acid Transporter Family;342
5.10.2.1.2;2.1.2 Amino Acid-Polyamine-Choline Transporter Family;343
5.10.2.2;2.2 Peptide Transporters;344
5.10.2.2.1;2.2.1 Peptide Transporter/Nitrate Transporter 1 Family;344
5.10.2.2.2;2.2.2 Oligopeptide Transporter Family;345
5.10.3;3 Sugar Transporters;346
5.10.3.1;3.1 Monosaccharide Transporters;346
5.10.3.1.1;3.1.1 Sugar Transport Protein Subfamily;346
5.10.3.1.2;3.1.2 Polyol Transporter Subfamily;348
5.10.3.1.3;3.1.3 Inositol Transporter Subfamily;348
5.10.3.1.4;3.1.4 Vacuolar Glucose Transporter-Like and Tonoplast Monosaccharide Transporter Subfamilies;348
5.10.3.2;3.2 Sucrose Transporters (SUTs or SUCs);349
5.10.3.2.1;3.2.1 Clade I (SUT1/SUC2);349
5.10.3.2.2;3.2.2 Clade II (SUT4);350
5.10.3.2.3;3.2.3 Clade III (SUT2);350
5.10.4;4 Conclusions;351
5.10.5;References;351
5.11;ABC Transporters and Their Function at the Plasma Membrane;361
5.11.1;1 ABC Transporters and Their Function;361
5.11.2;2 Structure and Evolution of Plant Plasma Membrane Transporters;362
5.11.3;3 The Nucleotide-Binding Fold: The Motor That Drives ABC Transport;364
5.11.4;4 The Two Halves of Full-Length ABC Transporters Are Similar But Not Identical;365
5.11.5;5 The Transmembrane Domain Forms the Pore and Functions as the Substrate Acceptor Site;366
5.11.6;6 The Transmembrane Helices Determine the Shape of the Pore;366
5.11.7;7 The Inner Lumen of the Transmembrane Barrel Determines Substrate Translocation;367
5.11.8;8 Substrate Translocation Mechanism Within the Transmembrane Domain;369
5.11.9;9 Membrane Insertion;369
5.11.10;10 Membrane Microdomains;370
5.11.11;11 Plant Plasma Membrane ABC Transporters: Two Subfamilies and Their Functions;371
5.11.11.1;11.1 ABCBs: Transport of Hormones, Organic Acids, and Alkaloids;371
5.11.11.2;11.2 Full-Length ABCG/PDR Proteins: At the Line of Plant Defense;376
5.11.11.3;11.3 ABCG/WBC Half-Transporters;377
5.11.12;12 Conclusions;378
5.11.13;References;379
5.12;Hormone Transport;386
5.12.1;1 Introduction;386
5.12.2;2 Known Transport Proteins for Phytohormones;387
5.12.2.1;2.1 Transporters for Auxins;387
5.12.2.2;2.2 Cytokinin Transporters;391
5.12.2.3;2.3 Abscisic Acid Transporters;392
5.12.2.4;2.4 Brassinosteroid Transport;393
5.12.2.5;2.5 Heterologous Expression of Phytohormone Transporters;393
5.12.2.6;2.6 Functional Characterization of Auxin Transporters;395
5.12.2.7;2.7 Computational and Mathematical Approaches to Understanding Phytohormone Transport;397
5.12.3;3 Conclusion;399
5.12.4;References;399
6;Section III Signal Transduction at the Plasma Membrane;405
6.1;Plant Hormone Perception at the Plasma Membrane;406
6.1.1;1 Introduction;406
6.1.2;2 Brassinosteroids;407
6.1.2.1;2.1 The PM-Localized Components of BR Signaling;409
6.1.2.2;2.2 The Cytosolic and Nuclear Components of BR Signaling;411
6.1.2.3;2.3 Proposed Mechanism of the Action of BR Perception and Signal Transduction;412
6.1.3;3 Cytokinin;413
6.1.3.1;3.1 The PM-Localized Components of Cytokinin Signaling;414
6.1.3.2;3.2 The Cytosolic and Nuclear Components of Cytokinin Signaling;416
6.1.3.2.1;3.2.1 The Phosphotransfer Proteins;416
6.1.3.2.2;3.2.2 The Response Regulators;416
6.1.3.3;3.3 Proposed Mechanism of Action of Cytokinin Perception and Signal Transduction;418
6.1.4;4 Abscisic Acid;418
6.1.5;5 Conclusion;421
6.1.6;References;422
6.2;Light Sensing at the Plasma Membrane;428
6.2.1;1 Phototropin Blue-Light Receptors;428
6.2.1.1;1.1 Phototropin Activity and Biological Functions;428
6.2.1.2;1.2 LOV Domains and Blue Light Sensing;430
6.2.1.3;1.3 Phototropin Activation and Phosphorylation;431
6.2.1.4;1.4 Phototropin Signaling at the PM;431
6.2.2;2 Additional Plant Blue Light Receptors;433
6.2.3;3 Phytochrome Red/Far-Red Light Receptors;433
6.2.4;4 UV-B and Green Light;434
6.2.5;5 Conclusions;435
6.2.6;References;436
6.3;The Hull of Fame: Lipid Signaling in the Plasma Membrane;442
6.3.1;1 The Role of the Plasma Membrane in Cell Signaling;442
6.3.1.1;1.1 The Phosphoinositide Pathway;443
6.3.2;2 PIs and the Plasma Membrane;444
6.3.2.1;2.1 Interaction of Soluble PI-Pathway Enzymes with the Plasma Membrane;445
6.3.3;3 PIs and the Regulation of Tip Growth;446
6.3.4;4 PI Control of Ion Channels;448
6.3.5;5 PIs and Plant Stress Responses;449
6.3.6;6 Sphingolipids in Plant Signaling;450
6.3.7;7 Conclusions;453
6.3.8;References;454
6.4;Plasma Membrane and Abiotic Stress;461
6.4.1;1 Plasma Membrane Abiotic Stress Sensing;461
6.4.2;2 PM Targets of Abiotic Stress Signals;464
6.4.3;3 Stomatal Guard Cells and Stress Responses at the PM;466
6.4.4;4 Membrane-Bound Transcription Factor and Response to Abiotic Stress;467
6.4.5;5 Other Posttranslational Regulation of PM Proteins;469
6.4.6;6 Abiotic Stress and Effects on PM Integrity;470
6.4.7;7 Conclusion;470
6.4.8;References;470
6.5;The Role of the Plant Plasma Membrane in Microbial Sensing and Innate Immunity;475
6.5.1;1 Introduction;475
6.5.2;2 Signals Activating Plant Immunity-Associated Defenses;476
6.5.2.1;2.1 Pathogen-Associated Molecular Patterns;476
6.5.2.2;2.2 Damage-Associated Molecular Patterns;478
6.5.2.3;2.3 Microbial Toxins as Triggers of Plant Defenses;479
6.5.3;3 Plasma Membrane Pattern Recognition Receptors in Plant Immunity;480
6.5.4;4 Auxiliary Factors Mediating Pattern Recognition Receptor Function;481
6.5.5;5 Suppression of PRR Function: A Major Virulence Strategy of Phytopathogenic Bacteria;482
6.5.6;References;484
7;Index;488