| The Secretory Pathway: From History to the State of the Art / Cordula Harter ; Constanze ReinhardChapter 1： |
| Summary / 1.： |
| Definition of the Secretory Pathway / 2.： |
| Discovery / 2.1.： |
| Stations of the Secretory Pathway / 2.2.： |
| Endoplasmic Reticulum / 2.2.1.： |
| ER-Golgi Intermediate Compartment / 2.2.2.： |
| The Golgi Apparatus / 2.2.3.： |
| Transport through the Secretory Pathway / 3.： |
| Export from the ER / 3.1.： |
| COPII-Coated Vesicles / 3.1.1.： |
| Transport into and through the Golgi / 3.2.： |
| COPI-Coated Vesicles / 3.2.1.： |
| Sorting at the trans-Golgi Network / 3.3.： |
| Clathrin-Coated Vesicles / 3.3.1.： |
| Recycling Pathways / 3.4.： |
| Membrane Proteins in Vesicle Formation and Cargo Selection / 3.5.： |
| Membrane Proteins of COP-Coated Vesicles / 3.5.1.： |
| Membrane Proteins of Clathrin-Coated Vesicles / 3.5.2.： |
| Mechanism of Vesicle Formation: Insights from the COPI System / 4.： |
| Bivalent Interaction of Coatomer / 4.1.： |
| Reconstitution of Coated Vesicles from Chemically Defined Liposomes / 4.2.： |
| Polymerization of Coatomer and COPI Bud Formation / 4.3.： |
| Mechanism of Vesicle Fusion / 5.： |
| SNARE Proteins / 5.1.： |
| NSF / 5.2.： |
| Additional Proteins Involved in Vesicle Fusion / 5.3.： |
| Targeting Proteins / 5.3.1.： |
| Modulators of SNARE Action / 5.3.2.： |
| Perspectives / 6.： |
| References / 7.： |
| Neurotoxins as Tools in Dissecting the Exocytic Machinery / Michal LinialChapter 2： |
| Introduction |
| The Core of the Exocytic Machinery--the SNAREs / 1.1.： |
| Direct Associates of SNAREs / 1.2.： |
| Dynamic View of Secretion / 1.3.： |
| Latrotoxin and Related Toxins |
| Biology of the Toxins--Cell Recognition |
| Structure and Biochemical Properties |
| Clostridial Toxins |
| Biology of the Toxins--Cell Recognition and Activation |
| Investigating Secretion with Clostridial Toxins--The Methodologies |
| In vivo--Genetic Approach |
| In vitro--Tissues and Cells |
| In vitro--Overexpressed Proteins |
| Clostridial Toxins as Molecular Probes for Secretion |
| Probes for Evolutionary Conservation and Diversity |
| Probes for Structural Specificity |
| Identifying New SNAREs, Their Associates and Their Roles |
| Studying the Diversity of Secretory Systems / 5.4.： |
| Clostridial Toxins as Therapeutic Tools |
| A Clinical Perspective / 6.1.： |
| In Model Systems / 6.2.： |
| Future Perspective |
| Annexins and Membrane Fusion / Helmut Kubista ; Sandra Sacre ; Stephen E. Moss8.： |
| Annexins in Membrane Fusion |
| The Structural Basis of Annexin-Membrane Interactions |
| Modulation of Annexin-Membrane Interactions by Phosphorylation |
| Annexins and Membrane Fusion in Exocytosis / 2.3.： |
| A Membrane Fusion Protein Activated by Ca[superscript 2+], GTP and Protein Kinase C / 2.3.1.： |
| Docking of Secretory Granules to the Plasma Membrane by Annexins / 2.3.2.： |
| Annexins and Vesicle Aggregation / 2.3.3.： |
| Annexins and the Organization of Membrane Microdomains / 2.3.4.： |
| Annexins as Membrane Fusogens / 2.3.5.： |
| Annexin-Mediated Ion Fluxes in Exocytosis / 2.3.6.： |
| Annexin Binding to Secretory Regulators / 2.3.7.： |
| Annexins and Membrane Fusion in Endocytosis |
| Annexin VI |
| Annexin II |
| Annexin I |
| Phagocytosis |
| Association of Annexins with Phagosomes |
| Annexin I and Phagocytosis in Neutrophils and Macrophages |
| The Annexin Family in Neutrophil Phagocytosis |
| Annexins in Regulated Exocytosis |
| Annexins from Simple Organisms |
| Annexin I in Exocytosis |
| Annexin II in Exocytosis |
| Annexin III in Exocytosis |
| Annexin V in Exocytosis / 5.5.： |
| Annexin VI in Exocytosis / 5.6.： |
| Annexin VII in Exocytosis / 5.7.： |
| Annexin XIII in Exocytosis / 5.8.： |
| Evidence against a Role for Annexins in Vesicle Trafficking |
| Annexins: Fusogenic or Non-Fusogenic |
| Conclusion and Outlook |
| The Full Complement of Yeast Ypt/Rab-GTPases and Their Involvement in Exo- and Endocytic Trafficking / Martin Gotte ; Thomas Lazar ; Jin-San Yoo ; Dietrich Scheglmann ; Dieter Gallwitz9.： |
| The Ras-Superfamily |
| The Ypt Protein: Structure |
| The GTPase Cycle |
| Ypt GTPases and SNAREs: The Fusion Machinery |
| The Ypt Family One by One |
| Ypt1p |
| Ypt31p/Ypt32p |
| Sec4p / 6.3.： |
| Ypt51p/Ypt52p/Ypt53p / 6.4.： |
| Ypt7p / 6.5.： |
| Ypt6p / 6.6.： |
| Ypt10p / 6.7.： |
| Ypt11p / 6.8.： |
| How Few Ypt GTPases Are Enough? |
| Essential and Nonessential Ypt GTPases / 7.1.： |
| Redundancy among Ypt GTPases / 7.2.： |
| Ypt GTPases and Vesicular Trafficking Routes / 7.3.： |
| Possible Roles of Long-Chain Fatty Acyl-CoA Esters in the Fusion of Biomembranes / Nils Joakim Faergeman ; Tina Ballegaard ; Jens Knudsen ; Paul N. Black ; Concetta DiRussoChapter 5： |
| Biophysical Properties of Long-Chain Fatty Acyl-CoA Esters and Their Interaction with Biomembranes |
| Vesicle Trafficking |
| Assembly of Transport Vesicles |
| Fusion of Transport Vesicles |
| Long-Chain Fatty Acyl-CoA Esters as Cofactors for Vesicles Budding and Fusion |
| Palmitoylation of Proteins Involved in Membrane Trafficking |
| The Enzymology of Protein Palmitoylation |
| Palmitoylation and Membrane Fusion, Similarities Between Influenza Virus Hemagglutinin and SNAREs |
| A Putative Link Between Coat Assembly, Phospholipases, Protein Kinases and Acyl-CoA Esters / 4.4.： |
| Acyl-CoA-Dependent Lipid Remodeling in Vesicle Trafficking |
| Acyl-CoA and Vesicle Trafficking, Lessons from Yeast Mutants |
| Allosteric Effects of Long-Chain Acyl-CoA on Vesicle Trafficking |
| Acyl-CoA Regulation of Ion Fluxes |
| Intracellular Acyl-CoA Binding Proteins |
| Acyl-CoA Binding Protein |
| Fatty Acid Binding Protein and Sterol Carrier Protein-2 in Acyl-CoA Metabolism |
| In Vivo Regulation of Long-Chain Acyl-CoA Esters |
| Regulation of the Intracellular Acyl-CoA Concentration / 8.1.： |
| Regulation of Vesicle Trafficking In Vivo by Long-Chain Acyl-CoA Esters |
| Brefeldin A: Revealing the Fundamental Principles Governing Membrane Dynamics and Protein Transport / Catherine L. Jackson10.： |
| The Morphological Basis of Transport in the ER-GOLGI System |
| The Classic Models: Anterograde Vesicular Transport and Cisternal Maturation |
| The Three-Dimensional Structure of Intracellular Organelles and the Concept of Membrane Transformation |
| Regulated Forward Membrane Flux as the Driving Force for Anterograde Transport in the Exocytic Pathway |
| Morphological and Biochemical Effects of BFA |
| Early Studies of the Effects of BFA on the Secretory Pathway in Mammalian Cells |
| Conflicting Reports: Does the Golgi Disappear or Not? |
| The Effects of BFA in Yeast |
| The Effects of BFA on the Endocytic Pathway and Lysosomes: Fusion of Organelles within Systems and Traffic Jams |
| A Model to Explain the Morphological Effects of BFA |
| Molecular Effects of BFA |
| BFA Causes the Rapid Release of the COPI Coat from Golgi Membranes |
| BFA Inhibits Guanine Nucleotide Exchange on ARF |
| BFA Causes the Release of Many Golgi-Associated Proteins from Membranes |
| The Sec7 Domain Family of ARF Guanine Nucleotide Exchange Factors |
| Identification of Sec7 Domain Proteins as ARF Exchange Factors |
| Different Sec7 Domain Proteins have Different Sensitivities to BFA |
| Mechanism of Action of BFA: Stabilization of an Abortive ARF-GDP-Sec7 Domain Protein Complex |
| Conclusion |
| Membrane Fusion Events during Nuclear Envelope Assembly / Philippe Collas ; Dominic PocciaChapter 7： |
| Introduction: The Nuclear Envelope Is a Dynamic Structure |
| Assembly of the Nuclear Envelope Is a Multistep Process |
| Nuclear Reconstitution in Cell-Free Systems as Tools to Study Nuclear Envelope Assembly |
| Targeting and Binding of Nuclear Vesicles to Chromatin |
| Role of Lipophilic Structures (LSs) in Membrane Vesicle Binding to Chromatin |
| Distinct Membrane Vesicle Populations Contribute to the NE / 1.4.： |
| Fusion of Nuclear Vesicles |
| Sealing and Growth of the Nuclear Envelope |
| Fusion of the Bulk of Nuclear Vesicles / 2.1.1.： |
| LS-Vesicle Fusion / 2.1.2.： |
| A Retrograde Vesicular Transport Mechanism Implicated in Nuclear Vesicle Targeting to Chromatin and Fusion? |
| Assays for Nuclear Vesicle Fusion |
| Fluorescence Evidence of Fusion |
| Exclusion of High Molecular Weight Dextran from Nuclei |
| Electron Microscopic Assays to Monitor Nuclear Vesicle Fusion |
| Cytosolic and Nucleotide Requirements for Nuclear Vesicle Fusion / 2.4.： |
| Involvement of Small GTP-Binding Proteins in Nuclear Vesicle Dynamics |
| Nuclear Vesicle Fusion Requires GTP Hydrolysis |
| Early Evidence for a Putative Role of ARFs in Nuclear Vesicle Dynamics |
| Evidence for a Non-ARF GTPase Active in Nuclear Envelope Assembly |
| Analogies Between Nuclear Vesicle Fusion and Fusion Events in Intracellular Membrane Trafficking |
| Inhibition of Nuclear Vesicle Fusion with the Sulphydryl Modifier, N-Ethylmaleimide |
| Targeted Membrane Fusion Orchestrated by Components of the SNARE Hypothesis |
| A Role for p97 in Nuclear Envelope Assembly? |
| Implication of SNAREs in Nuclear Vesicle Targeting and Fusion: An Argument |
| A Role of Nuclear Ca[superscript 2+] in Nuclear Vesicle Fusion? |
| A Ca[superscript 2+] Store at the Nuclear Envelope |
| Generating Ca[superscript 2+] Signals in the Nucleus |
| Evidence for Nuclear Ca[superscript 2+]-Independent Nuclear Envelope Assembly |
| Nuclear Vesicle Fusion Requires Membrane-Associated Fusigenic Elements |
| Proteins Mediating Nuclear Membrane Fusion in Yeast Are Being Identified |
| Relevance of Kar Protein Homologues in Nuclear Vesicle Fusion |
| Transactions at the Peroxisomal Membrane / Ben Distel ; Ineke Braakman ; Ype Elgersma ; Henk F. TabakChapter 8： |
| The Isolation of Yeast Mutants Disturbed in Peroxisome Function |
| Impermeability of the Peroxisomal Membrane |
| Import of Proteins into Peroxisomes |
| Formation of Peroxisomal Membranes |
| The ER to Peroxisome Connection |
| Do Peroxisomes Possess Unique Features? |
| Technical Shortcomings in the Peroxisome Field |
| Outlook |
| Neurons, Chromaffin Cells and Membrane Fusion / Peter Partoens ; Dirk Slembrouck ; Hilde De Busser ; Peter F.T. Vaughan ; Guido A.F. Van Dessel ; Werner P. De Potter ; Albert R. LagrouChapter 9： |
| Biogenesis and Axonal Transport of LDV/Secretory Granules |
| Exocytosis from LDV/Secretory Granules |
| The Membrane Composition of Secretory Vesicles/LDV |
| The Role of the Cytoskeleton in Secretion from LDV |
| The Human Neuroblastoma SH-SY5Y as a Model to Study the Role of the Cytoskeleton in Secretion from LDV |
| Cytoskeletal and Vesicular Proteins and Exocytosis / 3.2.2.： |
| Candidate Target Proteins for PKC Substrates / 3.2.3.： |
| Control of Actin Dynamics / 3.2.4.： |
| The Regulation of Cytoskeleton by PKC / 3.2.5.： |
| MARCKS / 3.2.6.： |
| GAP-43 / 3.2.7.： |
| Role of MARCKS in PKC Enhancement of Secretion in SH-SY5Y / 3.2.8.： |
| Involvement of Isoprenylation/Carboxymethylation in Regulated Exocytosis |
| Role of Rab3 and Helper Proteins in Controlled Exocytosis |
| Processing of Proteins through Isoprenylation and Carboxymethylation / 3.3.2.： |
| Regulatory Function of Protein Prenylation/Carboxymethylation in Exocytosis and Other Cellular Processes / 3.3.3.： |
| Endocytosis of LDV/Secretory Vesicles |
| Reversibility in Fusion Protein Conformational Changes: The Intriguing Case of Rhabdovirus-Induced Membrane Fusion / Yves GaudinChapter 10： |
| General Introduction |
| Metastability of the Native Viral Membrane Fusion Glycoprotein Is General |
| Influenza HA as the Model Fusogenic Glycoprotein |
| General |
| Low pH-Induced HA Conformational Change |
| Irreversibility of the Fusogenic Structural Transition Is a Common Feature of Viral Membrane Fusion |
| The Case of Fusogenic Glycoproteins Activated by Proteolytic Cleavage |
| The Case of Uncleaved Fusogenic Glycoproteins |
| The Rhabdovirus Exception |
| The Rhabdovirus Family |
| The Rhabdovirus Glycoprotein / 3.1.2.： |
| Fusion Properties of Rhabdoviruses |
| Low pH-Induced Conformational Changes of Rhabdovirus G |
| One Protein, Three Conformational States |
| Identification of the Fusion Domain of Rhabdoviruses |
| Mutations Affecting G Conformational Changes |
| Role of the Fusion Inactive State / 3.3.4.： |
| Other Differences between Rhabdoviral G and Influenza Virus HA Conformational Changes / 3.3.5.： |
| Attempt to Reconcile the Data Obtained on Rhabdoviruses with those Obtained on other Viral Families |
| Existence of Reversible Steps in Fusogenic Glycoproteins Conformational Changes |
| How do Rhabdoviruses Overcome the High Energetic Barrier Encountered During Fusion? |
| Final Remarks / 4.3： |
| Specific Roles for Lipids in Virus Fusion and Exit: Examples from the Alphaviruses / Margaret Kielian ; Prodyot K. Chatterjee ; Don L. Gibbons ; Yanping E. LuChapter 11： |
| The Alphavirus Lifecycle |
| Virus Structure and Assembly |
| Virus Entry and Fusion |
| Endocytic Entry and Low pH-Triggered Fusion |
| In Vitro Fusion with Liposomes |
| Conformational Changes in the Virus Spike during Membrane Fusion |
| Virus Exit Pathway and Requirements |
| The Role of Cholesterol in the Alphavirus Lifecycle |
| Role of Cholesterol in Fusion |
| In Vitro Cholesterol Requirements |
| In Vivo Cholesterol Requirements |
| Role of Cholesterol in Virus Exit |
| The Role of Sphingolipid in Alphavirus Fusion |
| In Vitro Requirement for Sphingolipid in Virus-Membrane Fusion |
| Structural Features of Fusion-Permissive Sphingolipids |
| Mechanisms of Cholesterol and Sphingolipid Requirements in Alphavirus Fusion and Exit |
| The Role of Cholesterol and Sphingolipid in Fusogenic Spike Protein Conformational Changes |
| Alphavirus Mutants with Reduced Cholesterol Requirements |
| Sequences Involved in the Alphavirus Cholesterol Requirement / 5.2.1.： |
| Sequences Involved in the SFV Cholesterol Requirement / 5.2.1.1.： |
| Sequences Involved in the SIN Cholesterol Requirement / 5.2.1.2.： |
| Mechanism of the srf-3 Mutation / 5.2.2.： |
| Mechanism of Cholesterol in Virus Exit |
| Role of Specific Lipids in the Entry and Exit of Other Pathogens |
| The Role of Cholesterol in Bacterial Toxin-Membrane Interactions |
| Other Viruses that May Require Specific Lipids |
| Human Immunodeficiency Virus / 6.2.1.： |
| Mouse Hepatitis Virus / 6.2.2.： |
| Ebola Virus / 6.2.3.： |
| African Swine Fever Virus / 6.2.4.： |
| Sendai Virus / 6.2.5.： |
| Role of Cholesterol in Transport of Influenza Hemagglutinin / 6.2.6.： |
| Lipid Stalk Intermediates in Membrane Fusion Reactions |
| Cellular Fusion Proteins |
| Future Directions |
| Fusion Mediated by the HIV-1 Envelope Protein / Carrie M. McManus ; Robert W. DomsChapter 12： |
| Viral Components of Fusion |
| Env |
| Gp120 |
| Gp41 |
| Cellular Components of Fusion |
| CD4 |
| The Major HIV-1 Coreceptors |
| The Importance of CCR5 and CXCR4 In Vitro and In Vivo |
| Alternative HIV-1 Coreceptors |
| Envelope-Receptor Interactions |
| Env Determinants of Coreceptor Use |
| CCR5 Determinants |
| CXCR4 Determinants |
| Conformational Changes Resulting from Receptor Interactions |
| CD4-Independent Virus Infection |
| Implications for Therapeutic Intervention and Concluding Thoughts |
| Sulfhydryl Involvement in Fusion Mechanisms / David Avram SandersChapter 13： |
| Protein Thiols--An Introduction |
| Cysteine--A Special Residue |
| Oxidation and Reduction--Environment and Enzymatic Catalysis |
| Thiol and Disulfide Modification Reagents |
| Protein Thiols in Cellular Membrane Fusion |
| Identified Thiol-Reagent-Modified Proteins |
| N-ethylmaleimide-Sensitive Factor-NSF |
| Calpains |
| Experimental Systems with Thiol-Reagent- or Disulfide-Reagent-Modified Proteins of Unknown Identity |
| Frog Neuromuscular Junction |
| Mammalian Sperm-Egg Fusion |
| Insulin and Renin Secretion |
| Sea-Urchin Pronuclear Fusion during Fertilization / 2.2.4.： |
| Sea-Urchin Egg Cortical Granule Exocytosis / 2.2.5.： |
| Microsome Fusion / 2.2.6.： |
| Endocytosis / 2.2.7.： |
| Protein Thiols in Viral-Glycoprotein-Mediated Membrane Fusion and Virus Entry |
| Coronaviruses |
| Alphaviruses |
| Murine Leukemia Viruses |
| Other Retroviruses and Filoviruses |
| A Reconsideration of Alphavirus Entry / 3.6.： |
| Index |
図書
