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Structure and function of calcium release channels / edited by Irina I. Serysheva. — Amsterdam : Elsevier Academic Press, c2010. – (58.1551/C976/v.66) |
Contents
Contents
Contributors xi
Preface xv
Previous Volumes in Series xvii
SECTION 1 RYR Ca2+ RELEASE CHANNELS
CHAPTER 1 RyRs: Their Disposition， Frequency， and Relationships with Other Proteins of Calcium Release Units
I. Overview 3
II. Introduction 4
III. Cardiac CRUs 4
IV. CRUs in Skeletal and Invertebrate Body Muscles 8
V. Factors Affecting CRU Assembly in Skeletal and Cardiac Muscles 12
VI. Isoform-Specific Features of RyR Distribution 16
VII. Architecture of SR and T Tubule Membranes is Muscle- and Fiber-Type Specific References 22
CHAPTER 2 Electron Microscopy of Ryanodine Receptors
I. Overview 27
II. Introduction 28
III. Cryo-EM of Macromolecular Complexes 28
IV. Three-Dimensional Architecture of RyR as Determined by Cryo-EM 29
V. s-Helices in the TM Region and the Mechanism of Calcium Channel Gating 32
VI. Synergism of 3D Cryo-EM and Other Biophysical/Biochemical Techniques 34
VII. Outlook and Perspectives 40
References 42
CHAPTER 3 The Ryanodine Receptor Pore: is There a Consensus View?
I. Overview 49
II. Introduction 50
III. Ion Handling in RyR 51
IV. Where is the PFR in the RyR Channel? 53
V. Attempts to Identify the Structure of the RyR PFR 58
VI. Theoretical Approaches to Understanding the Mechanisms Underlying Ion Translocation and Discrimination in RyR 61
VII. Testing Physical and Theoretical Models of the RyR PFR by Residue Substitution
VIII. Concluding Remarks 64
References 64
CHAPTER 4 Regulation of RyR Channel Gating by Ca2+， Mg2+ and ATP
I. Overview 69
II. Introduction 70
III. RyR2 in Cardiac Contraction and Pacemaking 70
IV. Four Ca2+ Sensing Mechanisms for RyR2 71
V. Synergistic Ca2+-Activation via Cytoplasmic and Luminal Facing Binding Sites 74
VI. Channel Open Times and the Role of Ca2+ Feed-Through 76
VII. Three Mechanisms for Mg2+-Inhibition of RyR2 77
VIII. A Model for Ca2+ and Mg2+ Regulation of RyR2 80
IX. Adenine Neucleotides 82
X. Regulation of RyR2 in Cardiac E-C Coupling 84
XI. Concluding Remarks 86
References 87
CHAPTER 5 Regulation of Ryanodine Receptor Ion Channels Through Posttranslational Modifications
I. Overview 91
II. Introduction 92
III. RyR1 and RyR2 Phosphorylation 93
IV. RyR Modulation by Reactive Oxygen and Nitrogen Species 99
V. Conclusions 104
References 105
CHAPTER 6 Crosstalk via the Sarcoplasmic Gap: The DHPR-RyR Interaction
I. Overview 115
II. DHPR and RyR Arrangement in Skeletal and Cardiac Muscle Membranes--Basis for Differences in the EC Coupling Mechanism 116
III. Structural Domains Involved in skDHPR-RyR1 Interaction 119
IV. The Role of Intracellular Molecular Regions Besides the Cqs II-III Loop in skDHPR-RyR1 Interaction 126
V. Intracellular Molecular Regions of Cqs Involved in Tetrad Formation 128
VI. The Role of the Accessory skDHPR Subunits in Interaction with RyR1 128
VII. Conclusion 131
References 133
CHAPTER 7 Ryanodinopathies: RyR-Linked Muscle Diseases
I. Overview 139
II. Introduction 140
III. RyR1-Linked Diseases 142
IV. RyR2-Linked Diseases 153
V. Conclusions and Perspectives 158
References 160
SECTION 2 IP3R Ca2+ RELEASE CHANNELS
CHAPTER 8 3D Structure of IP3 Receptor
I. Overview 171
II. Introduction 172
III. Predicted Topology of IP3R Molecule 173
IV. Arrangement of IP3R in the Native Membrane 175
V. 3D Structure of IP3R by Electron Microscopy 176
VI. Crystal Structures of Isolated Domains 182
VII. Conformational Transitions in IP3R Channel 183
VIII. Future Outlook 185
References 186
CHAPTER 9 Molecular Architecture of the Inositol 1，4，5-Trisphosphate Receptor Pore
I. Overview 191
II. Introduction 192
III. The Transmembrane Domains 194
IV. The Ion Conduction Pore: Electrophysiologic Studies 197
V. The Ion Conduction Pore: Modeling Studies 202
References 204
CHAPTER 10 Adenophostins: High-Affinity Agonists of IP3 Receptors
I. Overview 209
II. Discovery and Initial Characterization of Adenophostins 210
III. Structure and Synthesis of Adenophostin 212
IV. Activation of IP3R by Adenophostin 216
V. Why does Adenophostin Bind to IP3R With High-Affinity? 220
VI. Is Adenophostin more than a Stable， High-Affinity Agonist of IP3R? 225
References 228
CHAPTER 11 Regulation of IP3R Channel Gating by Ca2+ and Ca2+ Binding Proteins
I. Overview 235
II. Introduction 236
III. Cytoplasmic Ca2+ Regulation of IP3R Channel Gating 237
IV. Ca2+ Binding Protein Regulation of IP3R Channel Gating 263
References 267
CHAPTER 12 Regulation of Inositol 1，4，5-Trisphosphate Receptors by Phosphorylation and Adenine Nucleotides
I. Overview 273
II. Regulation of IP3R by Phosphorylation 274
III. Regulation of IP3R by Adenine Nucleotides 283
References 292
CHAPTER 13 Role of Thiols in the Structure and Function of Inositol Trisphosphate Receptors
I. Overview 299
II. Introduction 300
III. Regulation of IP3R Function by Changes in Thiol Redox State 300
IV. Comparison of Thiol Regulation of IP3Rs and RyRs 308
V. Cysteine Residues as Probes of IP3R Structure 310
VI. Future Directions 314
References 315
CHAPTER 14 Inositol 1，4，5-Tripshosphate Receptor， Calcium Signaling， and Polyglutamine Expansion Disorders
I. Overview 323
II. Huntington's Disease， Spinocerebellar Ataxia Type 2， and Spinocerebellar Ataxia Type 3 324
III. Mutant Huntingtin Specifically Sensitizes IP3R1 to IP3 325
IV. Mutant Huntingtin Activates NR2B-Containing NMDA Receptors 326
V. Deranged Ca2+ Signaling and Apoptosis of HD MSN 329
VI. IP3R and Abnormal Ca2+ Signaling in SCA2 Neurons 330
VII. IP3R and Abnormal Ca2+ Signaling in SCA3 Neurons 332
VIII. Ca2+ Blockers and Perspectives for Clinical Intervention in HD and SCA Patients
References 335
