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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

10.3K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
15.8K
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

5.9K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
5.9K

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Related Experiment Video

Updated: Apr 26, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

10.6K

Variable cooperativity in SNARE-mediated membrane fusion.

Javier M Hernandez1, Alex J B Kreutzberger2, Volker Kiessling2

  • 1Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany; and.

Proceedings of the National Academy of Sciences of the United States of America
|August 6, 2014
PubMed
Summary

The number of SNARE complexes mediating membrane fusion varies with membrane curvature. Small liposomes require fewer SNARE complexes for fusion than large liposomes, indicating flexible SNARE cooperation.

Keywords:
exocytosisfusion intermediateliposome docking

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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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Related Experiment Videos

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SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes are essential for membrane fusion.
  • The exact number of SNARE complexes required for fusion has been debated, with estimates varying widely.

Purpose of the Study:

  • To investigate the role of membrane curvature and liposome size in SNARE complex-mediated membrane fusion.
  • To determine if there is a conserved number of SNARE complexes involved in fusion events.

Main Methods:

  • Reconstitution of liposomes with varying synaptobrevin densities.
  • Measurement of lipid mixing efficiency in small (∼40 nm) and large (∼100 nm) liposomes.
  • Analysis of SNARE complex assembly and cooperativity based on liposome size and curvature.

Main Results:

  • Lipid mixing efficiency was maximal with small liposomes containing only one synaptobrevin.
  • Large liposomes required 23-30 synaptobrevins for efficient lipid mixing.
  • The number of SNARE complexes involved varied significantly with membrane curvature and liposome size.

Conclusions:

  • There is no universally conserved number of SNARE complexes; it depends on membrane curvature.
  • SNARE complex assembly exhibits strong and weak cooperative coupling modes, implicating different fusion intermediates.
  • The plasticity of SNAREs to engage in different coupling modes is crucial for biological membrane fusion.