Fusion of Biological Membranes and Related Problems

Автор(ы):Hilderson H.
06.10.2007
Год изд.:2002
Описание: Membrane fusion and targetting 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. In this volume of the series Subcellular Biochemistry some aspects of fusion of biological membranes as well as related problems are presented. Although not complete, one will find 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.
Оглавление:
Fusion of Biological Membranes and Related Problems — обложка книги.
Chapter 1
The Secretory Pathway: From History to the State of the Art
Cordula Harter and Constanze Reinhard
  1. Summary [1]
  2. Definition of the Secretory Pathway [2]
    2.1. Discovery [2]
    2.2. Stations of the Secretory Pathway [3]
      2.2.1. Endoplasmic Reticulum [3]
      2.2.2. ER-Golgi Intermediate Compartment [3]
      2.2.3. The Golgi Apparatus [4]
  3. Transport through the Secretory Pathway [5]
    3.1. Export from the ER [6]
      3.1.1. COPII-Coated Vesicles [6]
    3.2. Transport into and through the Golgi [9]
      3.2.1. COPI-Coated Vesicles [9]
    3.3. Sorting at the trans-Golgi Network [12]
      3.3.1. Clathrin-CoatedVesicles [13]
    3.4. Recycling Pathways [14]
    3.5. Membrane Proteins in Vesicle Formation and Cargo Selection [15]
      3.5.1. Membrane Proteins of COP-Coated Vesicles [15]
      3.5.2. Membrane Proteins of Clathrin-Coated Vesicles [17]
  4. Mechanism of Vesicle Formation: Insights from the COPI System [18]
    4.1. Bivalent Interaction of Coatomer [18]
    4.2. Reconstitution of Coated Vesicles from Chemically Defined Liposomes [19]
    4.3. Polymerization of Coatomer and COPI Bud Formation [20]
  5. Mechanism of Vesicle Fusion [20]
    5.1. SNARE Proteins [21]
    5.2. NSF [23]
    5.3. Additional Proteins Involved in Vesicle Fusion [24]
      5.3.1. Targeting Proteins [24]
      5.3.2. Modulators of SNARE Action [25]
  6. Perspectives [26]
  7. References [27]
Chapter 2
Neurotoxins as Tools in Dissecting the Exocytic Machinery
Michal Linial
  1. Introduction [39]
    1.1. The Core of the Exocytic Machinery—the SNAREs [39]
    1.2. Direct Associates of SNAREs [40]
    1.3. Dynamic View of Secretion [42]
  2. Latrotoxin and Related Toxins [44]
    2.1. Biology of the Toxins—Cell Recognition [44]
    2.2. Structure and Biochemical Properties [45]
  3. Clostridial Toxins [47]
    3.1. Biology of the Toxins—Cell Recognition and Activation [47]
    3.2. Structure and Biochemical Properties [49]
  4. Investigating Secretion with Clostridial Toxins — The Methodologies [52]
    4.1. In vivo—Genetic Approach [52]
    4.2. In vitro—Tissues and Cells [53]
    4.3. In vitro—Overexpressed Proteins [55]
  5. Clostridial Toxins as Molecular Probes for Secretion [57]
    5.1. Probes for Evolutionary Conservation and Diversity [57]
    5.2. Probes for Structural Specificity [58]
    5.3. Identifying New SNAREs, Their Associates and Their Roles [60]
    5.4. Studying the Diversity of Secretory Systems [61]
  6. Clostridial Toxins as Therapeutic Tools [62]
    6.1. A Clinical Perspective [62]
    6.2. In Model Systems [62]
  7. Future Perspective [63]
  8. References [63]
Chapter 3
Annexing and Membrane Fusion
Helmut Kubista, Sandra Sacre, and Stephen E. Moss
  1. Introduction [73]
  2. Annexins in Membrane Fusion [74]
    2.1. The Structural Basis of Annexin-Membrane Interactions [74]
    2.2. Modulation of Annexin-Membrane Interactions by Phosphorylation [80]
    2.3. Annexins and Membrane Fusion in Exocytosis [81]
      2.3.1. A Membrane Fusion Protein Activated by Ca(?), GTP and Protein Kinase С [82]
      2.3.2. Docking of Secretory Granules to the Plasma Membrane by Annexins [83]
      2.3.3. Annexins and Vesicle Aggregation [84]
      2.3.4. Annexins and the Organization of Membrane Microdomains [85]
      2.3.5. Annexins as Membrane Fusogens [87]
      2.3.6. Annexin-Mediated Ion Fluxes in Exocyto [88]
      2.3.7. Annexin Binding to Secretory Regulators [90]
  3. Annexins and Membrane Fusion in Endocytosis [90]
    3.1. Annexin VI [92]
    3.2. Annexin II [96]
    3.3. Annexin I [98]
  4. Phagocytosis [100]
    4.1. Association of Annexins with Phagosomes [102]
    4.2. Annexin I and Phagocytosis in Neutrophils and Macrophages [103]
    4.3. The Annexin Family inNeutrophil Phagocytosis [106]
  5. Annexins in Regulated Exocytosis [107]
    5.1. Annexins from Simple Organisms [107]
    5.2. Annexin I in Exocytosis [107]
    5.3. Annexin II in Exocytosis [108]
    5.4. Annexin III in Exocytasis [110]
    5.5. Annexin V in Exocytosis [110]
    5.6. Annexin VI in Exocytosis [111]
    5.7. Annexin VII in Exocytosis [111]
    5.8. Annexin XIII in Exocytosis [112]
  6. Evidence against a Role for Annexins in Vesicle Trafficking [113]
  7. Annexins: Fusogenic or Non-Fusogenic [113]
  8. Conclusion and Outlook [118]
  9. References [121]
Chapter 4
The Full Camplement of Yeast Ypt/Rab-GTPases and Their Involvement in Exo- and Endocytic Trafficking
Martin Gotte, Thomas Lazar, Jin-San Yoo, Dietrich Scheglmann, and Dieter Gallwitz
  1. Introduction [133]
  2. The Ras-Superfamily [135]
  3. The Ypt Protein: Structure [136]
  4. The GTPase Cycle [139]
  5. Ypt GTPases and SNAREs: The Fusion Machinery [142]
  6. The Ypt Family One by One [145]
    6.1. Yptlp [145]
    6.2. Ypt31p/Ypt32p [147]
    6.3. Sec4p [148]
    6.4. Ypt51p/Ypt52p/Ypt53p [150]
    6.5. Ypt7p [152]
    6.6. Ypt6p [153]
    6.7. Ypt10p [155]
    6.8. Ypt11p [156]
  7. How Few Ypt GTPases Are Enough? [157]
    7.1. Essential and Nonessential Ypt GTPases [157]
    7.2. Redundancy among Ypt GTPases [158]
    7.3. Ypt GTPases and Vesicular Trafficking Routes [159]
  8. References [162]
Chapter 5
Possible Roles of Long-chain Fatty Acyl-CoA Esters in the Fusion of Biomembranes
Nils Joakim Faergeman, Tina Ballegaard, Jens Knudsen, Paul N. Black, and Concetta DiRusso
  1. Introduction [175]
  2. Biophysical Properties of Long-chain Fatty Acyl-CoA Esters and Their Interaction with Biomembranes [178]
  3. Vesicle Trafficking [179]
    3.1. Assembly of Transport Vesicles [179]
    3.2. Fusion of Transport Vesicles [181]
  4. Long-chain Fatty Acyl-CoA Esters as Cofactors for Vesicles Budding and Fusion [188]
    4.1. Palmitoylation of Proteins Involved in Membrane Trafficking [190]
    4.2. The Enzymology of Protein Palmitoylation [193]
    4.3. Palmitoylation and Membrane Fusion, Similarities Between Influenza Virus Hemagglutinin and SNAREs [195]
    4.4. A Putative Link Between Coat Assembly, Phospholipases, Protein Kinases and Acyl-CoA Esters [198]
  5. Acyl-CoA-Dependent Lipid Remodeling in Vesicle Trafficking [199]
    5.1. Acyl-CoA and Vesicle Trafficking, Lessons from Yeast Mutants [200]
  6. Allosteric Effects of Long-chain Acyl-CoA on Vesicle Trafficking [202]
    6.1. Acyl-CoA Regulation of Ion Fluxes [202]
  7. Intracellular Acyl-CoA Binding Proteins [203]
    7.1. Acyl-CoA Binding Protein [203]
    7.2. Fatty Acid Binding Protein and Sterol Carrier Protein-2 in Acyl-CoA Metabolism [205]
  8. In Vivo Regulation of Long-chain Acyl-CoA Esters [207]
    8.1. Regulation of the Intracellular Acyl-CoA Concentration [207]
  9. Regulation of Vesicle Trafficking In Vivo by Long-chain Acyl-CoA Esters [211]
  10. References [213]
Chapter 6
Brefeldin A: Revealing the Fundamental principles Governing Membrane Dynamics and Protein Transport
Catherine L. Jackson
  1. Introduction [233]
  2. The Morphological Basis of Transport in the ER-GOLGI System [235]
    2.1. The Classic Models: Anterograde Vesicular Transport and Cisternal Maturation [235]
    2.2. The Three-Dimensional Structure of Intracellular Organelles and the Concept of Membrane Transformation [236]
    2.3. Regulated Forward Membrane Flux as the Driving Force for Anterograde Transport in the Exocytic Pathway [238]
  3. Morphological and Biochemical Effects of BFA [242]
    3.1. Early Studies of the Effects of BFA on the Secretory Pathway in Mammalian Cells [242]
    3.2. Conflicting Reports: Does the Golgi Disappear or Not? [243]
    3.3. The Effects of BFA in Yeast [245]
    3.4. The Effects of BFA on the Endocytic Pathway and Lysosomes: Fusion of Organelles within Systems and Traffic Jams [246]
    3.5. A Model to Explain the Morphological Effects of BFA [247]
  4. Molecular Effects of BFA [249]
    4.1. BFA Causes the Rapid Release of the COPI Coat from Golgi Membranes [249]
    4.2. BFA Inhibits Guanine Nucleotide Exchange on ARF [250]
    4.3. BFA Causes the Release of Many Golgi-Associated Proteins from Membranes [251]
  5. The Sec? Domain Family of ARF Guanine Nucleotide Exchange Factors [253]
    5.1. Identification of Sec? Domain Proteins as ARF Exchange Factors [253]
    5.2. Different Sec? Domain Proteins have Different Sensitivities to BFA [256]
    5.3. Mechanism of Action of BFA: Stabilization of an Abortive ARF-GDP-Sec7 Domain Protein Complex [257]
  6. Conclusion [260]
  7. References [263]
Chapter 7
Membrane Fusion Events during Nuclear Envelope Assembly
Philippe Collas and Dominic Poccia
  Introduction: The Nuclear Envelope Is a Dynamic Structure [273]
  1. Assembly of the Nuclear Envelope Is a Multistep Process [275]
    1.1. Nuclear Reconstitution in Cell-Free Systems as Tools to Study Nuclear Envelope Assembly [275]
    1.2. Targeting and Binding of Nuclear Vesicles to Chromatin [277]
    1.3. Role of Lipophilic Structures (LSs) in Membrane Vesicle Binding to Chromatin [278]
    1.4. Distinct Membrane Vesicle Populations Contribute to the NE [279]
  2. Fusion of Nuclear Vesicles [281]
    2.1. Sealing and Growth of the Nuclear Envelope [281]
      2.1.1. Fusion of the Bulk of Nuclear Vesicles [281]
      2.1.2. LS-Vesicle Fusion [282]
    2.2. A Retrograde Vesicular Transport Mechanism Implicated in Nuclear Vesicle Targeting to Chromatin and Fusion? [283]
    2.3. Assays for Nuclear Vesicle Fusion [283]
      2.3.1. Fluorescence Evidence of Fusion [283]
      2.3.2. Exclusion of High Molecular Weight Dextran fromNuclei [284]
      2.3.3. Electron Microscopic Assays to Monitor Nuclear Vesicle Fusion [284]
    2.4. Cytosolic and Nucleotide Requirements for Nuclear Vesicle Fusion [287]
  3. Involvement of Small GTP-Binding Proteins in Nuclear Vesicle Dynamics [288]
    3.1. Nuclear Vesicle Fusion Requires GTP Hydrolysis [288]
    3.2. Early Evidence for a Putative Role of ARFs in Nuclear Vesicle Dynamics [288]
    3.3. Evidence for a Non-ARF GTPase Active in Nuclear Envelope Assembly [289]
  4. Analogies Between Nuclear Vesicle Fusion and Fusion Events in Intracellular Membrane Trafficking [290]
    4.1. Inhibition of Nuclear Vesicle Fusion with the Sulphydryl Modifier, 7V-Ethylmaleimide [290]
    4.2. Targeted Membrane Fusion Orchestrated by Components of the SNARE Hypothesis [291]
    4.3. A Role for p97 in Nuclear Envelope Assembly? [291]
    4.4. Implication of SNAREs in Nuclear Vesicle Targeting and Fusion: An Argument [292]
  5. A Role of Nuclear Ca(?) in Nuclear Vesicle Fusion? [293]
    5.1. A Ca(?) Store at the Nuclear Envelope [293]
    5.2. Generating Ca(?) Signals in the Nucleus [293]
    5.3. Evidence for Nuclear Ca(?)-Independent Nuclear Envelope Assembly [294]
  6. Nuclear Vesicle Fusion Requires Membrane Associated Fusigenic Elements [295]
    6.1. Proteins Mediating Nuclear Membrane Fusion in Yeast Are Being Identified [295]
    6.2. Relevance of Kar Protein Homologues in Nuclear Vesicle Fusion [296]
  7. References [296]
Chapter 8
Transactions at the P(?)eroxisomal Membrane
Ben Distel, Ineke Braakman, Ype Elgersma, and Henk F . Tabak
  1. Introduction [303]
  2. The Isolation of Yeast Mutants Disturbed in Peroxisome Function [305]
  3. Impermeability of the Peroxisomal Membrane [306]
  4. Import of Proteins into Peroxisomes [307]
  5. Formation of Peroxisomal Membranes [310]
  6. The ER to Peroxisome Connection [311]
  7. Do Peroxisomes Possess Unique Features? [314]
  8. Technical Shortcomings in the Peroxisome Field [315]
  9. Outlook [317]
  10. References [317]
Chapter 9
Neurons, Chromaffin Cells and Membrane Fusion
Peter Partoens Dirk Slembrouck, Hilde De Baser, Peter F. T. Vaughan, Euido A. F. Van Dessel, Werner P. De Potter, and Albert R. Lagrou
  1. Introduction [323]
  2. Biogenesis and Axonal Transport of LDV/Secretory Granules [326]
  3. Exocytosis from LDVlSecretory Granules [327]
    3.1. The Membrane Composition of Secretory Vesicles/LDV [327]
    3.2. The Role ofthe Cytoskeleton in Secretion from LDV [332]
      3.2.1. The Human Neuroblastoma SH-SY5Y as a Model to Study the Role ofthe Cytoskeleton in Secretion from LDV [332]
      3.2.2. Cytoskeletal and Vesicular Proteins and Exocytosis [334]
      3.2.3. Candidate Target Proteins for PKC Substrates [337]
      3.2.4. Control of Actin Dynamics [339]
      3.2.5. The Regulati]on of Cytoskeleton by PKC [340]
      3.2.6. MARCKS [343]
      3.2.7. GAP-43 [346]
      3.2.8. Role of MARCKS in PKC Enhancement of Secretion in SH-SY5Y [347]
    3.3. Involvement of Isoprenylation/Carboxymethylation in Regulated Exocytosis [348]
      3.3.1. Role of Rab3 and Helper Proteins in Controlled Exocytosis [348]
      3.3.2. Processing of Proteins through Isoprenylation and Carboxymethylation [355]
      3.3.3. Regulatory Function of Protein Prenylatiod Carboxymethylation in Exocytosis and Other Cellular Processes [358]
    4. Endocytosis of LDV/Secretory Vesicles [362]
    5. References [363]
Chapter 10
Reversibility in Fusion Protein Conformational Changes: The Intriguing Case of Rhabdovirus-Induced Membrane Fusion
Yves Gaudin
  1. General Introduction [379]
  2. Metastability of the Native Viral Membrane Fusion Glycoprotein Is General [381]
    2.1. Influenza HA as the Model Fusogenic Glycoprotein [381]
      2.1.1. General [381]
      2.1.2. Low pH-Induced HA Conformational Change [381]
    2.2. Irreversibility of the Fusogenic Structural Transition Is a Common Feature of Viral Membrane Fusion [383]
      2.2.1. The Case of Fusogenic Glycoproteins Activated by Proteolytic Cleavage [383]
      2.2.2. The Case of Uncleaved Fusogenic Glycoproteins [384]
  3. The Rhabdovirus Exception [385]
    3.1. The Rhabdovirus Family [385]
      3.1.1. General [385]
      3.1.2. The Rhabdovirus Glycoprotein [85]
    3.2. Fusion Properties of Rhabdoviruses [387]
    3.3. Low pH-Induced Conformational Changes of Rhabdovirus G [388]
      3.3.1. One Protein, Three Conformational States [388]
      3.3.2. Identification of the Fusion Domain of Rhabdoviruses [391]
      3.3.3. Mutations Affecting G Conformational Changes [394]
      3.3.4. Role of the Fusion Inactive State [395]
      3.3.5. Other Differences between Rhabdoviral G and Influenza Virus HA Conformational Changes [397]
  4. Attempt to Reconcile the Data Obtained on Rhabdoviruses with those Obtained on other Viral Families [398]
    4.1. Existence of Reversible Steps in Fusogenic Glycoproteins Conformational Changes [398]
    4.2. How do Rhabdoviruses Overcome the High Energetic Barrier Encountered During Fusion? [398]
    4.3. Final Remarks [401]
  5. References [401]
Chapter 11
Specific Roles for Lipids in Virus Fusion and Exit: Examples from the Alphaviruses
Margaret Kielian. Prodyot К . Chatterjee. Don L. Gibbons, and Yanping E. Lu
  1. Introduction [409]
  2. The Alphavirus Lifecycle [410]
    2.1. Virus Structure and Assembly [411]
    2.2. Virus Entry and Fusion [413]
      2.2.1. Endocytic Entry and Low pH-Triggered Fusion [413]
      2.2.2. In Vitro Fusion with Liposomes [416]
      2.2.3. Conformational Changes in the Virus Spike during Membrane Fusion [416]
    2.3. Virus Exit Pathway and Requirements [419]
  3. The Role of Cholesterol in the Alphavirus Lifecycle [420]
    3.1. Role of Cholesterol in Fusion [420]
      3.1.1. In Vitro Cholesterol Requirements [420]
      3.1.2. In Vivo Cholesterol Requirements [422]
    3.2. Role of Cholesterol in Vis Exit [423]
  4. The Role of Sphingolipid in Alphavirus Fusion [424]
    4.1. In Vitro Requirement for Sphingolipid in Virus-Membrane Fusion [424]
    4.2. Structural Features of Fusion-Permissive Sphingolipids [424]
  5 . Mechanisms of Cholesterol and Sphingolidpid Requirements in Alphavirus Fusion and Exit [425]
    5.1. The Role of Cholesterol and Sphingolipid in Fusogenic Spike Protein Conformational Changes [425]
    5.2. Alphavirus Mutants with Reduced Cholesterol Requirements [427]
      5.2.1. Sequences Involved in, the Alphavirus Cholesterol Requirement [427]
        5.2.1.1. Sequences Involved in the SFV Cholesterol Requirement [427]
        5.2.1.2. Sequences Involved in the SIN Cholesterol Requirement [430]
      5.2.2. Mechanism of the srf-3 Mutation [431
    5.3. Mechanism of Cholesterol in Virus Exit [432]
  6. Role of Specifc Lipids in the Entry and Exit of Other Pathogens [432]
    6.1. The Role of Cholesterol in Bacterial Toxin-Membrane Interactions [433]
    6.2. Other Viruses that May Require Specific Lipids [435]
      6.2.1. Human Immunodeficiency Virus [435]
      6.2.2. Mouse Hepatitis Virus [437]
      6.2.3. Ebola Virus [438]
      6.2.4. African Swine Fever Virus [439]
      6.2.5. Seadai virus [440]
      6.2.6. Role of Cholesterol in Transport of Influenza Hemagglutinin [441]
    6.3. Lipid Stalk Intermediates in Membrane Fusion Reactions [442]
    6.4. Cellular Fusion Proteins [443]
  7. Future Directions [445]
  8. References [446]
Chapter 12
Fusion Mediated by the HIV-1 Envelope Protein
Carrie M. McManus and Robert W. Doms
  1. Introduction [457]
  2. Viral Components of Fusion [458]
    2.1. Env [458]
      2.1.1. Gpl20 [458]
      2.1.2. Gp41 [460]
  3. Cellular Components of Fusion [462]
    3.1. CD4 [462]
    3.2. The Major HIV-1 Coreceptors [462]
      3.2.1. The Importance of CCR5 and CXCR4 In Vitro and In Vivo [464]
    3.3. Alternative HIV-1 Coreceptors [465]
  4. Envelope-Receptor Interactions [466]
    4.1. Env Determinants of Coreceptor Use [467]
    4.2. CCR5 Determinants [468]
    4.3. CXCR4 Determinants [469]
    4.4. Conformational Changes Resulting from Receptor Interactions [469]
  5. CD4-Independent Virus Infection [470]
  6. Implications for Therapeutic .Intervention and Concluding Thoughts [471]
  7. References [472]
Chapter 13
Sulfhdryl Involvement in Fusion Mechanisms
David Avram Sanders
  1. Protein Thiols—An Introduction [483]
    1.1. Cysteine—A Special Residue [483]
    1.2. Oxidation and Reduction—Environment and Enzymatic Catalysis [484]
    1.3. Thiol and Bisulfide Modification Reagents [486]
  2. Protein Thiols in Cellular Membrane Fusion [489]
    2.1. Identified Thiol-Reagent-Modified Proteins [489]
      2.1.1. Ж-ethylmakimide-Sensitive Factor-NSF [489]
      2.1.2. Calpains [490]
    2.2. Experimental Systems with Thiol-Reagent- or Disulfide-Reagent-Modified Proteins of Unknown Identity [491]
      2.2.1. Frog Neuromuscular Junction [491]
      2.2.2. Mammalian Sperm-Egg Fusion [491]
      2.2.3. Insulin and Renin Secretion [492]
      2.2.4. Sea-Urchin Pronuclear Fusion during Fertilization [493]
      2.2.5. Sea-Urchin Egg Cortical Granule Exocytosis [493]
      2.2.6. Microsome Fusion [494]
      2.2.7. Endocytosis [495]
  3. Protein Thiols in Viral-Glycoprotein-Mediated Membrane Fusion and Virus Entry [496]
    3.1. Human Immunodeficiency Virus [496]
    3.2. Coronaviruses [497]
    3.3. Alphaviruses [498]
    3.4. Murine Leukemia Viruses [501]
    3.5. Other Retroviruses and Filoviruses [507]
    3.6. A Reconsideration of Alphavirus Entry [508]
  4. Conclusion [509]
  5. References [509]
Index [515]
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