Krebs Membrane Dynamics and Calcium Signaling

1. Auflage 2018
ISBN: 978-3-319-55858-5
Verlag: Springer International Publishing
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 981, 409 Seiten

Reihe: Advances in Experimental Medicine and Biology

This book describes the newest discoveries on calcium signaling happening at the cellular and intracellular membranes, often exerted in so called microdomains. Calcium entry and release, its interaction with proteins and resulting events on proteins and organelles are comprehensively depicted by leading experts in the field. Knowledge about details of these highly dynamic processes rapidly increased in recent years, the book therefore provides a timely summary on the processes of calcium signaling and related membrane dynamics; it is aimed at students and researchers in biochemistry and cell biology.

Prof. Joachim Krebs is Prof. Emeritus of the Swiss federal Institute of Technology (ETH) ; at present he is Consultant at the MPI for Biophysical Chemistry, Department on NMR-based Structural Biology, Göttingen, Germany. Prof. Krebs was working for more than 30 years in the field of calcium signaling, calcium-binding and calcium-transport proteins and has importantly contributed to the understanding of calcium function and signaling pathways in the cell.

Autoren/Hrsg.

Krebs, Joachim

Inhaltsverzeichnis

1;Preface;6
2;Contents;8
3;Part I: Plasma Membrane;10
3.1;Chapter 1: The Plasma Membrane Calcium Pump (PMCA): Regulation of Cytosolic Ca2+, Genetic Diversities and Its Role in Sub-plas...;11
3.1.1;1.1 Introduction;11
3.1.2;1.2 General Properties of PMCA;13
3.1.3;1.3 Structural Details of PMCA;15
3.1.4;1.4 Genetic Diversity of PMCA in Health and Disease;17
3.1.4.1;1.4.1 PMCA1;18
3.1.4.2;1.4.2 PMCA2;20
3.1.4.3;1.4.3 PMCA3;21
3.1.4.4;1.4.4 PMCA4;21
3.1.5;1.5 PMCA and Microdomains of Ca2+ Signaling;22
3.1.6;1.6 Conclusions;23
3.1.7;References;24
3.2;Chapter 2: Structure-Function Relationship of the Voltage-Gated Calcium Channel Cav1.1 Complex;30
3.2.1;2.1 Introduction;31
3.2.1.1;2.1.1 Classification of Voltage-Gated Calcium Channels;31
3.2.1.2;2.1.2 Molecular Properties of Cav;32
3.2.1.3;2.1.3 Channelopathies;33
3.2.2;2.2 Structural Studies of Voltage-Gated Calcium Channels;33
3.2.3;2.3 Structural Analysis of Cav1.1;35
3.2.3.1;2.3.1 The Overall Architecture of Cav1.1;35
3.2.3.2;2.3.2 Structure of the ?1 Subunit;35
3.2.3.3;2.3.3 The VSDs of Cav1.1;36
3.2.3.4;2.3.4 The Selectivity Filter;37
3.2.3.5;2.3.5 The Auxiliary Subunits;39
3.2.3.6;2.3.6 Structural Mapping of Disease-Associated Mutations;40
3.2.4;2.4 Voltage-Gated Calcium Channels in Excitation-Contraction Coupling;40
3.2.5;2.5 Perspective;43
3.2.6;References;43
3.3;Chapter 3: Structure-Dynamic Coupling Through Ca2+-Binding Regulatory Domains of Mammalian NCX Isoform/Splice Variants;47
3.3.1;3.1 Ca2+ Sensing by Isoform/Splice Variants and Multitask Ca2+ Signaling;48
3.3.2;3.2 Structural and Regulatory Specificities of NCX Isoform/Splice Variants;48
3.3.2.1;3.2.1 Coordination Chemistry Controls the Number and Affinity of Ca2+ Sites in Uniformly Folded CBDs;49
3.3.2.2;3.2.2 Each CBD Domain Plays a Distinct Regulatory Role;50
3.3.2.3;3.2.3 Exon Arrays Differentially Control the Tissue-Specific Regulatory Modes of NCX Variants;51
3.3.3;3.3 Synergistic Interactions Between CBDs Control the Ca2+ Sensing Features;53
3.3.3.1;3.3.1 CBD12 Crystal Structures Highlight the Functional Significance of the Two-Domain Interface;54
3.3.3.2;3.3.2 Ca2+ Dependent Rigidification Underlies Dynamic Coupling of CBDs;57
3.3.4;3.4 Structure-Dynamic Basis for Ca2+ Evoked Decoding of Regulatory Massage;57
3.3.5;3.5 Exon-Specific Roles in Editing the Regulatory Massage;58
3.3.6;3.6 Conclusions;60
3.3.7;References;61
4;Part II: Endoplasmic/Sarcoplasmic Reticulum;65
4.1;Chapter 4: The Endoplasmic Reticulum and the Cellular Reticular Network;66
4.1.1;4.1 Introduction;67
4.1.2;4.2 The ER;67
4.1.3;4.3 ER and Ca2+ Homeostasis;69
4.1.4;4.4 ER-Plasma Membrane Connection: Store-Operated Calcium Entry;69
4.1.5;4.5 ER and Protein Quality Control;71
4.1.6;4.6 ER and Cellular Stress Coping Response Strategies;71
4.1.7;4.7 ER and Lipid Metabolism;72
4.1.8;4.8 ER and Membrane Contact Sites;74
4.1.9;4.9 Conclusions;75
4.1.10;References;76
4.2;Chapter 5: Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin;82
4.2.1;5.1 Calcium Homeostasis;82
4.2.2;5.2 SERCA Isoforms and Human Disease (P-Type ATPases);83
4.2.2.1;5.2.1 SERCA1;83
4.2.2.2;5.2.2 SERCA2;84
4.2.2.3;5.2.3 SERCA3;85
4.2.3;5.3 Catalytic Cycle of Calcium Transport by SERCA;86
4.2.4;5.4 Structural Studies of SERCA;88
4.2.4.1;5.4.1 Structural Insights into the SERCA Calcium Transport Cycle;90
4.2.5;5.5 Regulation of SERCA by Phospholamban;92
4.2.5.1;5.5.1 Introduction to Phospholamban;92
4.2.5.2;5.5.2 Oligomerization of Phospholamban and the Theory of Mass Action;94
4.2.5.3;5.5.3 SERCA Inhibition by Phospholamban;96
4.2.5.4;5.5.4 Structural Studies of Phospholamban and SERCA/Phospholamban Complex;98
4.2.5.5;5.5.5 Regulation of Phospholamban;100
4.2.5.6;5.5.6 Phospholamban in Heart Failure;102
4.2.5.6.1;5.5.6.1 Arg9-Cys (R9C);102
4.2.5.6.2;5.5.6.2 Arg14-Deletion (R14del);104
4.2.5.6.3;5.5.6.3 Arg9-Leu (R9L) and Arg9-His (R9H);105
4.2.5.6.4;5.5.6.4 Leu39-Stop (L39stop);106
4.2.5.6.5;5.5.6.5 Arg25-Cys (R25C);106
4.2.5.6.6;5.5.6.6 Mutations in the Promoter and Intronic Regions;107
4.2.6;5.6 Regulation of SERCA by Sarcolipin;107
4.2.6.1;5.6.1 Introduction to Sarcolipin;107
4.2.6.2;5.6.2 Regulatory Mechanism of SERCA Inhibition by Sarcolipin;107
4.2.6.3;5.6.3 Structure of Sarcolipin;108
4.2.6.4;5.6.4 Oligomeric State of Sarcolipin;109
4.2.6.5;5.6.5 Sarcolipin Physically Interacts with SERCA;110
4.2.6.6;5.6.6 Role of Sarcolipin in the Heart;112
4.2.6.7;5.6.7 Sarcolipin Regulates Thermogenesis in Skeletal Muscle;114
4.2.7;5.7 Targeting SERCA Regulatory Complexes as Therapy for Cardiac Disease;114
4.2.8;5.8 Future Directions for SERCA Regulation;116
4.2.9;References;116
4.3;Chapter 6: Structural Insights into IP3R Function;125
4.3.1;6.1 Introduction;126
4.3.2;6.2 Historical Perspective on the Structural Studies of IP3R;127
4.3.3;6.3 Validation of the 3D Structure of IP3R;130
4.3.4;6.4 Near-Atomic Resolution Structure of Tetrameric IP3R Assembly;131
4.3.5;6.5 Structure-Function Conservation in Ca2+ Release Channel Family;140
4.3.6;6.6 Conclusions and Future Perspective;144
4.3.7;References;147
4.4;Chapter 7: IP3 Receptor Properties and Function at Membrane Contact Sites;152
4.4.1;7.1 The IP3 Receptor, the Main Ca2+-Release Channel of the Endoplasmic Reticulum;154
4.4.2;7.2 Mitochondrial and Lysosomal Ca2+ Handling in Cell Death and Survival Processes;157
4.4.2.1;7.2.1 Apoptosis and Its Regulation by Ca2+;157
4.4.2.2;7.2.2 Autophagy and Its Regulation by Ca2+;158
4.4.3;7.3 The Role of the IP3R at ER: Mitochondrial Contact Sites;159
4.4.3.1;7.3.1 IP3R-Mediated Ca2+ Signals in Cell Survival;161
4.4.3.2;7.3.2 IP3R-Mediated Ca2+ Signals in Apoptosis;164
4.4.4;7.4 The Role of the IP3R at ER: Lysosomal Contact Sites;165
4.4.5;7.5 Conclusions;167
4.4.6;References;168
4.5;Chapter 8: Structural Details of the Ryanodine Receptor Calcium Release Channel and Its Gating Mechanism;182
4.5.1;8.1 Introduction;182
4.5.2;8.2 Structure of RyR;186
4.5.3;8.3 Gating of RyR;193
4.5.4;8.4 Regulation of Gating;196
4.5.5;8.5 RyR in Diseases;198
4.5.6;8.6 Conclusions;201
4.5.7;References;201
4.6;Chapter 9: Store-Operated Calcium Entry: An Historical Overview;208
4.6.1;References;214
4.7;Chapter 10: From Stores to Sinks: Structural Mechanisms of Cytosolic Calcium Regulation;218
4.7.1;10.1 Calcium Signaling;219
4.7.2;10.2 N-Terminal Domain of IP3R;222
4.7.2.1;10.2.1 IP3-Induced Receptor Activation;224
4.7.2.2;10.2.2 Allosteric Regulation of Channel Gating by IP3;226
4.7.3;10.3 STIM1/2 EF-SAM Structure and Function;229
4.7.3.1;10.3.1 STIM1 Coiled-Coil Domain Structure and Function;232
4.7.3.2;10.3.2 Drosophila melanogaster Orai Crystal Structure and Function;234
4.7.3.3;10.3.3 STIM1 Coupling to Orai1;236
4.7.4;10.4 MCU Structure and Function;238
4.7.4.1;10.4.1 MCU N-Terminal Domain Structure and Function;240
4.7.5;10.5 Concluding Remarks;242
4.7.6;References;244
4.8;Chapter 11: Assembly of ER-PM Junctions: A Critical Determinant in the Regulation of SOCE and TRPC1;255
4.8.1;11.1 Introduction;256
4.8.2;11.2 The Molecular Components of SOCE;257
4.8.3;11.3 Regulation of TRPC1 Following ER-Ca2+ Depletion;261
4.8.4;11.4 Plasma Membrane Domains in Regulation of SOCE;263
4.8.5;11.5 PMCA, SERCA and Ca2+ Signaling Microdomains;266
4.8.6;11.6 The Role of Lipid Raft Domains in the Regulation of TRPC1;267
4.8.7;11.7 Conclusions;269
4.8.8;References;269
5;Part III: Mitochondria;279
5.1;Chapter 12: Beyond Intracellular Signaling: The Ins and Outs of Second Messengers Microdomains;280
5.1.1;12.1 Introduction;281
5.1.2;12.2 The Microdomain Concept;282
5.1.3;12.3 Ca2+ Microdomains;283
5.1.4;12.4 Ca2+ Microdomains at the ER-Mitochondria Interface: Generation and Functional Significance;288
5.1.5;12.5 Heterogeneity of Ca2+ Levels Within Organelles;292
5.1.5.1;12.5.1 ER/SR;292
5.1.5.2;12.5.2 Golgi Apparatus;295
5.1.5.3;12.5.3 Mitochondria;295
5.1.6;12.6 cAMP Microdomains;296
5.1.6.1;12.6.1 The Generation of cAMP Microdomains;297
5.1.6.2;12.6.2 cAMP Effectors;298
5.1.6.3;12.6.3 cAMP Generation;299
5.1.6.4;12.6.4 cAMP Degradation;300
5.1.6.5;12.6.5 Termination of cAMP Signaling;301
5.1.7;12.7 Ca2+ and cAMP Crosstalk;302
5.1.8;12.8 ATP Microdomains;305
5.1.9;12.9 Other Microdomains;309
5.1.10;12.10 Conclusions;309
5.1.11;References;310
5.2;Chapter 13: Mitochondrial VDAC, the Na+/Ca2+ Exchanger, and the Ca2+ Uniporter in Ca2+ Dynamics and Signaling;324
5.2.1;13.1 Overview;325
5.2.2;13.2 Mitochondria and Ca2+ Dynamics;325
5.2.3;13.3 Ca2+ Transporters in the Mitochondria;325
5.2.3.1;13.3.1 VDAC1: The Ca2+ Transporter in the OMM;326
5.2.3.1.1;13.3.1.1 VDAC1 Structure, Channel Conductance, Properties, and Regulation;326
5.2.3.1.2;13.3.1.2 VDAC1, a Multifunctional Channel Controlling Cell Metabolism;327
5.2.3.1.3;13.3.1.3 VDAC1 a Ca2+ Channel in the OMM;327
5.2.3.2;13.3.2 Ca2+ Transporters and Their Regulation in the IMM;329
5.2.3.2.1;13.3.2.1 MCU and Its Regulatory Proteins;329
5.2.3.2.2;13.3.2.2 Other Ca2+ Influx Pathways;330
5.2.3.3;13.3.3 Ca2+ Efflux Out of Mitochondria;330
5.2.3.3.1;13.3.3.1 NCLX Mediating Ca2+ Efflux;331
5.2.3.3.2;13.3.3.2 Other Proteins That have been Proposed to Mediate Ca2+ Efflux from Mitochondria;331
5.2.4;13.4 Mitochondria Ca2+, VDAC1 and Regulation of Metabolism;332
5.2.5;13.5 Mitochondrial Ca2+, VDAC1 and Regulation of Apoptosis;333
5.2.6;13.6 VDAC1 Function in ER/Mitochondria-Ca2+ Cross-Talk;334
5.2.7;13.7 microRNA Mediated Regulation of Mitochondrial Ca2+ Transporters and Channels;335
5.2.7.1;13.7.1 miRNAs Regulate VDAC1;335
5.2.7.2;13.7.2 miRNAs Regulate the MCU Complex;336
5.2.8;13.8 Defects of Other Mitochondrial Proteins in Ca2+ Homeostasis and Diseases;336
5.2.8.1;13.8.1 Diabetes;336
5.2.8.2;13.8.2 Cancer;336
5.2.8.3;13.8.3 Other Diseases;337
5.2.9;References;337
6;Part IV: Annexins;349
6.1;Chapter 14: Annexins: Ca2+ Effectors Determining Membrane Trafficking in the Late Endocytic Compartment;350
6.1.1;14.1 Introduction;351
6.1.2;14.2 Annexins: Ca2+ Binding and Ca2+ Sensitivity;352
6.1.2.1;14.2.1 Annexin A6: Location, Signalling and Dynamics;353
6.1.3;14.3 Intracellular Ca2+ Stores and Ca2+-Binding Proteins;355
6.1.3.1;14.3.1 Ca2+ in Acidic Compartments;358
6.1.3.2;14.3.2 Ca2+ and Annexins in the Endo- and Exocytic Pathways;360
6.1.4;14.4 Ca2+ Signalling and the Biogenesis, Function and Positioning of Acidic Compartments;362
6.1.4.1;14.4.1 Intra-Endosomal Trafficking: ILV Back-Fusion in MVBs;363
6.1.4.2;14.4.2 Lysosomal Exocytosis: A Selective Ca2+ Pathway;364
6.1.4.3;14.4.3 Ca2+ and Ca2+ Binding Proteins in Membrane Repair;366
6.1.4.3.1;14.4.3.1 Annexins: Masters in Membrane Repair;367
6.1.4.4;14.4.4 Ca2+ and Annexins Regulate Lysosomal Positioning;369
6.1.5;14.5 Concluding Remarks;370
6.1.6;References;371
7;Part V: Cytokinesis and Ca2+ Signaling;385
7.1;Chapter 15: Ca2+ Signalling and Membrane Dynamics During Cytokinesis in Animal Cells;386
7.1.1;15.1 Introduction;387
7.1.1.1;15.1.1 Historical Perspective;387
7.1.1.2;15.1.2 General Aspects of Cytokinesis;388
7.1.2;15.2 The Cytokinetic Ca2+ Transients;389
7.1.2.1;15.2.1 Generation of Distinct Ca2+ Transients During Cytokinesis;389
7.1.2.2;15.2.2 Identifying the Source of Ca2+ Generating Cytokinetic Transients;392
7.1.2.2.1;15.2.2.1 Positioning and Propagation Ca2+ Transients;393
7.1.2.2.2;15.2.2.2 Deepening and Apposition Ca2+ Transients;394
7.1.3;15.3 Possible Targets of the Cytokinetic Ca2+ Transients;395
7.1.3.1;15.3.1 The Positioning and Propagation Ca2+ Transients;395
7.1.3.2;15.3.2 The Deepening and Apposition Ca2+ Transients;399
7.1.4;15.4 Conclusions;403
7.1.5;References;404