Standard Article

Membrane Fusion

Handbook of Physiology, Cell Physiology

  1. R. Blumenthal,
  2. D. S. Dimitrov

Published Online: 1 JAN 2011

DOI: 10.1002/cphy.cp140114

Comprehensive Physiology

Comprehensive Physiology

How to Cite

Blumenthal, R. and Dimitrov, D. S. 2011. Membrane Fusion. Comprehensive Physiology. 563–603.

Author Information

  1. Section on Membrane Structure and Function, National Cancer Institute, National Institutes of Health, Bethesda, Maryland

Publication History

  1. Published Online: 1 JAN 2011

Abstract

The sections in this article are:

  • 1
    Observation of Fusion Requires Physical Techniques for Monitoring Mixing of Membranes and the Compartments they Enclose
    • 1.1
      Morphological Changes Following Fusion Are Observed by Light Microscopy but Membrane Fusion May Occur without such Changes
    • 1.2
      Fluorescence Microscopy and Spectrofluorometry Allow Quantitation of Membrane Fusion Events in Living Cells
    • 1.3
      Electron Microscopy Provides Direct Observation of Structural Rearrangements Due to Fusion
    • 1.4
      Patch-Clamp Techniques Allow the Monitoring of Very Fast Openings of Fusion Pores
  • 2
    What Do We Learn from “Nonbiological” Fusion Processes?
    • 2.1
      Ca2+ Induces Aggregation Destabilization, and Fusion of Liposomes Containing Phospholipids with Negatively Charged Head-groups
    • 2.2
      Fusion of Lipid Membranes by Amphipathic and Nonpolar Molecules Correlates with Their Lytic and Aggregational Activity
    • 2.3
      Dehydration, Aggregation, and Destabilization of Membranes by Polyethelene Glycol Are Essential for Fusion of Lipid Membranes
    • 2.4
      Destabilization by High-Voltage Electric Pulses Leads to Fusion of Adjoining Membranes
    • 2.5
      Molecular Rearrangements in the Lipid Bilayers during the Very Act of Fusion May Involve Intermediate Structures
  • 3
    Specialized Proteins Mediate Fusion in Life Processes
  • 4
    Viral Envelope Proteins Contain Hydrophobic “Fusion Peptide” Sequences
    • 4.1
      To Enter a Cell a Virus Must Find the Receptor That Invites It In
    • 4.2
      Some Viruses Require More Than One Type of Envelope Protein for Entry
    • 4.3
      Influenza Hemagglutinin Was the Only Fusion Protein with Known Three-Dimensional Structure
    • 4.4
      The Process of HA-mediated Membrane Fusion Can Be Dissected into a Number of Elementary Steps
    • 4.5
      Human Immunodeficiency Virus Type 1 (HIV-1), the Primary Etiological Agent of the Acquired Immunodeficiency Syndrome (AIDS), Enters Cells by Membrane Fusion at Neutral pH
    • 4.6
      The Receptor CD4 Plays Both a Passive and an Active Role in Allowing Entry of the Virus into the Cell
    • 4.7
      Stable Envelope Glycoprotein-Receptor Complex Formation Is Rate-limiting in the Overall Fusion Process
    • 4.8
      Multiple Copies of the HIV-1 Envelope Glycoprotein May Be Required for Fusion Pore Formation
  • 5
    Sperm Membrane Proteins Involved in Sperm-Egg Fusion May Resemble Viral Fusion Proteins
  • 6
    Toward A Resolution of Fusion Proteins in Exocytosis
  • 7
    Multiple Proteins May Be Required for Intracellular Fusion
  • 8
    Toward A Physicochemical Analysis of Fusion Kinetics
    • 8.1
      Delays in Fusion Are Proportional to the Fusion Barriers and Decrease with an Increase in the Strength of the Fusogen
    • 8.2
      Rates of Fusion Can Provide Information for the Time Course of Membrane Merging and Fusion Pore Expansion
    • 8.3
      Fusion Yields and Delays Are Related but May Reflect Different Properties of the Fusing Membranes
  • 9
    Does Understanding Membrane Fusion Need New Breakthroughs in Methodology?
  • 10
    Note Added in Proof