+612 9045 4394
$7.95 Delivery per order to Australia and New Zealand
100% Australian owned
Over a hundred thousand in-stock titles ready to ship
Fusion of Biological Membranes and Related Problems : Subcellular Biochemistry - Herwig J. Hilderson

Fusion of Biological Membranes and Related Problems

Subcellular Biochemistry

By: Herwig J. Hilderson (Editor), Stephen Fuller (Editor)

Hardcover Published: 1st April 2000
ISBN: 9780306463136
Number Of Pages: 529

Share This Book:


or 4 easy payments of $118.72 with Learn more
Ships in 10 to 15 business days

Earn 950 Qantas Points
on this Book

Other Available Editions (Hide)

  • Paperback View Product Published: 19th November 2010
    Ships in 10 to 15 business days

Membrane fusion and targeting processes are tightly regulated and coordinated. Dozens of proteins, originating from both the cytoplasm and membranes are involved. The discovery of homologous proteins from yeast to neurons validates a unified view.
Although much is known about the interfering proteins, the events occurring when two lipid bilayers actually fuse are less clear. It should be remembered that lipid bilayers behave like soap-bubbles fusing when meeting each other. In this respect interfering proteins should be considered as preventing undesirable and unnecessary fusion and eventually directing the biological membrane fusion process (when, where, how, and overcoming the activation energy).
In this latest volume in the renowned Subcellular Biochemistry series, some aspects of fusion of biological membranes as well as related problems are presented. Although not complete, there is a lot of recent information including on virus-induced membrane fusion. The contributors of the chapters are all among the researchers who performed many of the pioneering studies in the field.

The Secretory Pathway: From History to the State of the Art
Summaryp. 1
Definition of the Secretory Pathwayp. 2
Discoveryp. 2
Stations of the Secretory Pathwayp. 3
Endoplasmic Reticulump. 3
ER-Golgi Intermediate Compartmentp. 3
The Golgi Apparatusp. 4
Transport through the Secretory Pathwayp. 5
Export from the ERp. 6
COPII-Coated Vesiclesp. 6
Transport into and through the Golgip. 9
COPI-Coated Vesiclesp. 9
Sorting at the trans-Golgi Networkp. 12
Clathrin-Coated Vesiclesp. 13
Recycling Pathwaysp. 14
Membrane Proteins in Vesicle Formation and Cargo Selectionp. 15
Membrane Proteins of COP-Coated Vesiclesp. 15
Membrane Proteins of Clathrin-Coated Vesiclesp. 17
Mechanism of Vesicle Formation: Insights from the COPI Systemp. 18
Bivalent Interaction of Coatomerp. 18
Reconstitution of Coated Vesicles from Chemically Defined Liposomesp. 19
Polymerization of Coatomer and COPI Bud Formationp. 20
Mechanism of Vesicle Fusionp. 20
SNARE Proteinsp. 21
NSFp. 23
Additional Proteins Involved in Vesicle Fusionp. 24
Targeting Proteinsp. 24
Modulators of SNARE Actionp. 25
Perspectivesp. 26
Referencesp. 26
Neurotoxins as Tools in Dissecting the Exocytic Machinery
Introductionp. 39
The Core of the Exocytic Machinery--the SNAREsp. 39
Direct Associates of SNAREsp. 40
Dynamic View of Secretionp. 42
Latrotoxin and Related Toxinsp. 44
Biology of the Toxins--Cell Recognitionp. 44
Structure and Biochemical Propertiesp. 45
Clostridial Toxinsp. 47
Biology of the Toxins--Cell Recognition and Activationp. 47
Structure and Biochemical Propertiesp. 49
Investigating Secretion with Clostridial Toxins--The Methodologiesp. 52
In vivo--Genetic Approachp. 52
In vitro--Tissues and Cellsp. 53
In vitro--Overexpressed Proteinsp. 55
Clostridial Toxins as Molecular Probes for Secretionp. 57
Probes for Evolutionary Conservation and Diversityp. 57
Probes for Structural Specificityp. 58
Identifying New SNAREs, Their Associates and Their Rolesp. 60
Studying the Diversity of Secretory Systemsp. 61
Clostridial Toxins as Therapeutic Toolsp. 62
A Clinical Perspectivep. 62
In Model Systemsp. 62
Future Perspectivep. 63
Referencesp. 63
Annexins and Membrane Fusion
Introductionp. 73
Annexins in Membrane Fusionp. 74
The Structural Basis of Annexin-Membrane Interactionsp. 74
Modulation of Annexin-Membrane Interactions by Phosphorylationp. 80
Annexins and Membrane Fusion in Exocytosisp. 81
A Membrane Fusion Protein Activated by Ca[superscript 2+], GTP and Protein Kinase Cp. 82
Docking of Secretory Granules to the Plasma Membrane by Annexinsp. 83
Annexins and Vesicle Aggregationp. 84
Annexins and the Organization of Membrane Microdomainsp. 85
Annexins as Membrane Fusogensp. 87
Annexin-Mediated Ion Fluxes in Exocytosisp. 88
Annexin Binding to Secretory Regulatorsp. 90
Annexins and Membrane Fusion in Endocytosisp. 90
Annexin VIp. 92
Annexin IIp. 96
Annexin Ip. 98
Phagocytosisp. 100
Association of Annexins with Phagosomesp. 102
Annexin I and Phagocytosis in Neutrophils and Macrophagesp. 103
The Annexin Family in Neutrophil Phagocytosisp. 106
Annexins in Regulated Exocytosisp. 107
Annexins from Simple Organismsp. 107
Annexin I in Exocytosisp. 107
Annexin II in Exocytosisp. 108
Annexin III in Exocytosisp. 110
Annexin V in Exocytosisp. 110
Annexin VI in Exocytosisp. 111
Annexin VII in Exocytosisp. 111
Annexin XIII in Exocytosisp. 112
Evidence against a Role for Annexins in Vesicle Traffickingp. 113
Annexins: Fusogenic or Non-Fusogenicp. 113
Conclusion and Outlookp. 118
Referencesp. 121
The Full Complement of Yeast Ypt/Rab-GTPases and Their Involvement in Exo- and Endocytic Trafficking
Introductionp. 133
The Ras-Superfamilyp. 135
The Ypt Protein: Structurep. 136
The GTPase Cyclep. 139
Ypt GTPases and SNAREs: The Fusion Machineryp. 142
The Ypt Family One by Onep. 145
Ypt1pp. 145
Ypt31p/Ypt32pp. 147
Sec4pp. 148
Ypt51p/Ypt52p/Ypt53pp. 150
Ypt7pp. 152
Ypt6pp. 153
Ypt10pp. 155
Ypt11pp. 156
How Few Ypt GTPases Are Enough?p. 157
Essential and Nonessential Ypt GTPasesp. 157
Redundancy among Ypt GTPasesp. 158
Ypt GTPases and Vesicular Trafficking Routesp. 159
Referencesp. 162
Possible Roles of Long-Chain Fatty Acyl-CoA Esters in the Fusion of Biomembranes
Introductionp. 175
Biophysical Properties of Long-Chain Fatty Acyl-CoA Esters and Their Interaction with Biomembranesp. 178
Vesicle Traffickingp. 179
Assembly of Transport Vesiclesp. 179
Fusion of Transport Vesiclesp. 181
Long-Chain Fatty Acyl-CoA Esters as Cofactors for Vesicles Budding and Fusionp. 188
Palmitoylation of Proteins Involved in Membrane Traffickingp. 190
The Enzymology of Protein Palmitoylationp. 193
Palmitoylation and Membrane Fusion, Similarities Between Influenza Virus Hemagglutinin and SNAREsp. 195
A Putative Link Between Coat Assembly, Phospholipases, Protein Kinases and Acyl-CoA Estersp. 198
Acyl-CoA-Dependent Lipid Remodeling in Vesicle Traffickingp. 199
Acyl-CoA and Vesicle Trafficking, Lessons from Yeast Mutantsp. 200
Allosteric Effects of Long-Chain Acyl-CoA on Vesicle Traffickingp. 202
Acyl-CoA Regulation of Ion Fluxesp. 202
Intracellular Acyl-CoA Binding Proteinsp. 203
Acyl-CoA Binding Proteinp. 203
Fatty Acid Binding Protein and Sterol Carrier Protein-2 in Acyl-CoA Metabolismp. 205
In Vivo Regulation of Long-Chain Acyl-CoA Estersp. 207
Regulation of the Intracellular Acyl-CoA Concentrationp. 207
Regulation of Vesicle Trafficking In Vivo by Long-Chain Acyl-CoA Estersp. 211
Referencesp. 213
Brefeldin A: Revealing the Fundamental Principles Governing Membrane Dynamics and Protein Transport
Introductionp. 233
The Morphological Basis of Transport in the ER-GOLGI Systemp. 235
The Classic Models: Anterograde Vesicular Transport and Cisternal Maturationp. 235
The Three-Dimensional Structure of Intracellular Organelles and the Concept of Membrane Transformationp. 236
Regulated Forward Membrane Flux as the Driving Force for Anterograde Transport in the Exocytic Pathwayp. 238
Morphological and Biochemical Effects of BFAp. 242
Early Studies of the Effects of BFA on the Secretory Pathway in Mammalian Cellsp. 242
Conflicting Reports: Does the Golgi Disappear or Not?p. 243
The Effects of BFA in Yeastp. 245
The Effects of BFA on the Endocytic Pathway and Lysosomes: Fusion of Organelles within Systems and Traffic Jamsp. 246
A Model to Explain the Morphological Effects of BFAp. 247
Molecular Effects of BFAp. 249
BFA Causes the Rapid Release of the COPI Coat from Golgi Membranesp. 249
BFA Inhibits Guanine Nucleotide Exchange on ARFp. 250
BFA Causes the Release of Many Golgi-Associated Proteins from Membranesp. 251
The Sec7 Domain Family of ARF Guanine Nucleotide Exchange Factorsp. 253
Identification of Sec7 Domain Proteins as ARF Exchange Factorsp. 253
Different Sec7 Domain Proteins have Different Sensitivities to BFAp. 256
Mechanism of Action of BFA: Stabilization of an Abortive ARF-GDP-Sec7 Domain Protein Complexp. 257
Conclusionp. 260
Referencesp. 263
Membrane Fusion Events during Nuclear Envelope Assembly
Introduction: The Nuclear Envelope Is a Dynamic Structurep. 273
Assembly of the Nuclear Envelope Is a Multistep Processp. 275
Nuclear Reconstitution in Cell-Free Systems as Tools to Study Nuclear Envelope Assemblyp. 275
Targeting and Binding of Nuclear Vesicles to Chromatinp. 277
Role of Lipophilic Structures (LSs) in Membrane Vesicle Binding to Chromatinp. 278
Distinct Membrane Vesicle Populations Contribute to the NEp. 279
Fusion of Nuclear Vesiclesp. 281
Sealing and Growth of the Nuclear Envelopep. 281
Fusion of the Bulk of Nuclear Vesiclesp. 281
LS-Vesicle Fusionp. 282
A Retrograde Vesicular Transport Mechanism Implicated in Nuclear Vesicle Targeting to Chromatin and Fusion?p. 283
Assays for Nuclear Vesicle Fusionp. 283
Fluorescence Evidence of Fusionp. 283
Exclusion of High Molecular Weight Dextran from Nucleip. 284
Electron Microscopic Assays to Monitor Nuclear Vesicle Fusionp. 284
Cytosolic and Nucleotide Requirements for Nuclear Vesicle Fusionp. 287
Involvement of Small GTP-Binding Proteins in Nuclear Vesicle Dynamicsp. 288
Nuclear Vesicle Fusion Requires GTP Hydrolysisp. 288
Early Evidence for a Putative Role of ARFs in Nuclear Vesicle Dynamicsp. 288
Evidence for a Non-ARF GTPase Active in Nuclear Envelope Assemblyp. 289
Analogies Between Nuclear Vesicle Fusion and Fusion Events in Intracellular Membrane Traffickingp. 290
Inhibition of Nuclear Vesicle Fusion with the Sulphydryl Modifier, N-Ethylmaleimidep. 290
Targeted Membrane Fusion Orchestrated by Components of the SNARE Hypothesisp. 291
A Role for p97 in Nuclear Envelope Assembly?p. 291
Implication of SNAREs in Nuclear Vesicle Targeting and Fusion: An Argumentp. 292
A Role of Nuclear Ca[superscript 2+] in Nuclear Vesicle Fusion?p. 293
A Ca[superscript 2+] Store at the Nuclear Envelopep. 293
Generating Ca[superscript 2+] Signals in the Nucleusp. 293
Evidence for Nuclear Ca[superscript 2+]-Independent Nuclear Envelope Assemblyp. 294
Nuclear Vesicle Fusion Requires Membrane-Associated Fusigenic Elementsp. 295
Proteins Mediating Nuclear Membrane Fusion in Yeast Are Being Identifiedp. 295
Relevance of Kar Protein Homologues in Nuclear Vesicle Fusionp. 296
Referencesp. 296
Transactions at the Peroxisomal Membrane
Introductionp. 303
The Isolation of Yeast Mutants Disturbed in Peroxisome Functionp. 305
Impermeability of the Peroxisomal Membranep. 306
Import of Proteins into Peroxisomesp. 307
Formation of Peroxisomal Membranesp. 310
The ER to Peroxisome Connectionp. 311
Do Peroxisomes Possess Unique Features?p. 314
Technical Shortcomings in the Peroxisome Fieldp. 315
Outlookp. 317
Referencesp. 317
Neurons, Chromaffin Cells and Membrane Fusion
Introductionp. 323
Biogenesis and Axonal Transport of LDV/Secretory Granulesp. 326
Exocytosis from LDV/Secretory Granulesp. 327
The Membrane Composition of Secretory Vesicles/LDVp. 327
The Role of the Cytoskeleton in Secretion from LDVp. 332
The Human Neuroblastoma SH-SY5Y as a Model to Study the Role of the Cytoskeleton in Secretion from LDVp. 332
Cytoskeletal and Vesicular Proteins and Exocytosisp. 334
Candidate Target Proteins for PKC Substratesp. 337
Control of Actin Dynamicsp. 339
The Regulation of Cytoskeleton by PKCp. 340
MARCKSp. 343
GAP-43p. 346
Role of MARCKS in PKC Enhancement of Secretion in SH-SY5Yp. 347
Involvement of Isoprenylation/Carboxymethylation in Regulated Exocytosisp. 348
Role of Rab3 and Helper Proteins in Controlled Exocytosisp. 348
Processing of Proteins through Isoprenylation and Carboxymethylationp. 355
Regulatory Function of Protein Prenylation/Carboxymethylation in Exocytosis and Other Cellular Processesp. 358
Endocytosis of LDV/Secretory Vesiclesp. 362
Referencesp. 363
Reversibility in Fusion Protein Conformational Changes: The Intriguing Case of Rhabdovirus-Induced Membrane Fusion
General Introductionp. 379
Metastability of the Native Viral Membrane Fusion Glycoprotein Is Generalp. 381
Influenza HA as the Model Fusogenic Glycoproteinp. 381
Generalp. 381
Low pH-Induced HA Conformational Changep. 381
Irreversibility of the Fusogenic Structural Transition Is a Common Feature of Viral Membrane Fusionp. 383
The Case of Fusogenic Glycoproteins Activated by Proteolytic Cleavagep. 383
The Case of Uncleaved Fusogenic Glycoproteinsp. 384
The Rhabdovirus Exceptionp. 385
The Rhabdovirus Familyp. 385
Generalp. 385
The Rhabdovirus Glycoproteinp. 385
Fusion Properties of Rhabdovirusesp. 387
Low pH-Induced Conformational Changes of Rhabdovirus Gp. 388
One Protein, Three Conformational Statesp. 388
Identification of the Fusion Domain of Rhabdovirusesp. 391
Mutations Affecting G Conformational Changesp. 394
Role of the Fusion Inactive Statep. 395
Other Differences between Rhabdoviral G and Influenza Virus HA Conformational Changesp. 397
Attempt to Reconcile the Data Obtained on Rhabdoviruses with those Obtained on other Viral Familiesp. 398
Existence of Reversible Steps in Fusogenic Glycoproteins Conformational Changesp. 398
How do Rhabdoviruses Overcome the High Energetic Barrier Encountered During Fusion?p. 398
Final Remarksp. 401
Referencesp. 401
Specific Roles for Lipids in Virus Fusion and Exit: Examples from the Alphaviruses
Introductionp. 409
The Alphavirus Lifecyclep. 410
Virus Structure and Assemblyp. 411
Virus Entry and Fusionp. 413
Endocytic Entry and Low pH-Triggered Fusionp. 413
In Vitro Fusion with Liposomesp. 416
Conformational Changes in the Virus Spike during Membrane Fusionp. 416
Virus Exit Pathway and Requirementsp. 419
The Role of Cholesterol in the Alphavirus Lifecyclep. 420
Role of Cholesterol in Fusionp. 420
In Vitro Cholesterol Requirementsp. 420
In Vivo Cholesterol Requirementsp. 422
Role of Cholesterol in Virus Exitp. 423
The Role of Sphingolipid in Alphavirus Fusionp. 424
In Vitro Requirement for Sphingolipid in Virus-Membrane Fusionp. 424
Structural Features of Fusion-Permissive Sphingolipidsp. 424
Mechanisms of Cholesterol and Sphingolipid Requirements in Alphavirus Fusion and Exitp. 425
The Role of Cholesterol and Sphingolipid in Fusogenic Spike Protein Conformational Changesp. 425
Alphavirus Mutants with Reduced Cholesterol Requirementsp. 427
Sequences Involved in the Alphavirus Cholesterol Requirementp. 427
Sequences Involved in the SFV Cholesterol Requirementp. 427
Sequences Involved in the SIN Cholesterol Requirementp. 430
Mechanism of the srf-3 Mutationp. 431
Mechanism of Cholesterol in Virus Exitp. 432
Role of Specific Lipids in the Entry and Exit of Other Pathogensp. 432
The Role of Cholesterol in Bacterial Toxin-Membrane Interactionsp. 433
Other Viruses that May Require Specific Lipidsp. 435
Human Immunodeficiency Virusp. 435
Mouse Hepatitis Virusp. 437
Ebola Virusp. 438
African Swine Fever Virusp. 439
Sendai Virusp. 440
Role of Cholesterol in Transport of Influenza Hemagglutininp. 441
Lipid Stalk Intermediates in Membrane Fusion Reactionsp. 442
Cellular Fusion Proteinsp. 443
Future Directionsp. 445
Referencesp. 446
Fusion Mediated by the HIV-1 Envelope Protein
Introductionp. 457
Viral Components of Fusionp. 458
Envp. 458
Gp120p. 458
Gp41p. 460
Cellular Components of Fusionp. 462
CD4p. 462
The Major HIV-1 Coreceptorsp. 462
The Importance of CCR5 and CXCR4 In Vitro and In Vivop. 464
Alternative HIV-1 Coreceptorsp. 465
Envelope-Receptor Interactionsp. 466
Env Determinants of Coreceptor Usep. 467
CCR5 Determinantsp. 468
CXCR4 Determinantsp. 469
Conformational Changes Resulting from Receptor Interactionsp. 469
CD4-Independent Virus Infectionp. 470
Implications for Therapeutic Intervention and Concluding Thoughtsp. 471
Referencesp. 472
Sulfhydryl Involvement in Fusion Mechanisms
Protein Thiols--An Introductionp. 483
Cysteine--A Special Residuep. 483
Oxidation and Reduction--Environment and Enzymatic Catalysisp. 484
Thiol and Disulfide Modification Reagentsp. 486
Protein Thiols in Cellular Membrane Fusionp. 489
Identified Thiol-Reagent-Modified Proteinsp. 489
N-ethylmaleimide-Sensitive Factor-NSFp. 489
Calpainsp. 490
Experimental Systems with Thiol-Reagent- or Disulfide-Reagent-Modified Proteins of Unknown Identityp. 491
Frog Neuromuscular Junctionp. 491
Mammalian Sperm-Egg Fusionp. 491
Insulin and Renin Secretionp. 492
Sea-Urchin Pronuclear Fusion during Fertilizationp. 493
Sea-Urchin Egg Cortical Granule Exocytosisp. 493
Microsome Fusionp. 494
Endocytosisp. 495
Protein Thiols in Viral-Glycoprotein-Mediated Membrane Fusion and Virus Entryp. 496
Human Immunodeficiency Virusp. 496
Coronavirusesp. 497
Alphavirusesp. 498
Murine Leukemia Virusesp. 507
Other Retroviruses and Filovirusesp. 507
A Reconsideration of Alphavirus Entryp. 508
Conclusionp. 509
Referencesp. 509
Indexp. 515
Table of Contents provided by Syndetics. All Rights Reserved.

ISBN: 9780306463136
ISBN-10: 030646313X
Series: Subcellular Biochemistry
Audience: General
Format: Hardcover
Language: English
Number Of Pages: 529
Published: 1st April 2000
Publisher: Springer Science+Business Media
Country of Publication: US
Dimensions (cm): 23.39 x 15.6  x 3.02
Weight (kg): 0.95

Earn 950 Qantas Points
on this Book

This product is categorised by