Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Addendum: In situ architecture of the human prohibitin complex.

Nature cell biology·2026
Same author

Catestatin restores cardiac metabolic flexibility and enhances mitochondrial function.

Communications biology·2026
Same author

RNA promotes synapsin phase separation providing a platform for local translation.

bioRxiv : the preprint server for biology·2026
Same author

Multi-Network Co-expression Analysis Enhances Biological Insights from Single-Cell Gene Expression.

Interdisciplinary sciences, computational life sciences·2026
Same author

Membrane-protein-mediated phase separation orchestrates organelle contact sites.

Molecular cell·2026
Same author

What Is the Role of Giant Endosomal Sorting Complexes Required for Transport (ESCRT) Structures in T Cell Activation?

Advanced biology·2025

Related Experiment Video

Updated: Jun 16, 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

One SNARE complex is sufficient for membrane fusion.

Geert van den Bogaart1, Matthew G Holt, Gertrude Bunt

  • 1Department of Neurobiology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.

Nature Structural & Molecular Biology
|February 9, 2010
PubMed
Summary

One SNARE complex is sufficient for membrane fusion, challenging previous assumptions. This finding suggests that multiple SNARE complexes do not need to work together for membrane fusion events.

More Related Videos

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

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

Published on: October 19, 2012

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Related Experiment Videos

Last Updated: Jun 16, 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

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

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

Published on: October 19, 2012

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Area of Science:

  • Cell biology
  • Molecular biology
  • Biophysics

Background:

  • Intracellular membrane fusion in eukaryotes relies on SNARE proteins.
  • The minimum number of SNARE complexes required for fusion is unknown.

Purpose of the Study:

  • To determine the minimal number of SNARE complexes necessary for membrane fusion.
  • To investigate the cooperative behavior of SNARE complexes during fusion.

Main Methods:

  • Controlled in vitro Förster resonance energy transfer (FRET) experiments.
  • Liposome-based assays with single SNARE molecules.
  • Fusion assays with purified synaptic vesicles.

Main Results:

  • A single SNARE complex is sufficient to mediate membrane fusion.
  • Liposomes with one SNARE molecule fused with other liposomes and synaptic vesicles.
  • Multiple SNARE complexes do not exhibit cooperative or synergistic effects.

Conclusions:

  • Revises the understanding of SNARE-mediated membrane fusion mechanisms.
  • Suggests that single SNARE complexes drive fusion events.
  • Impacts the comprehension of processes like neurotransmitter release.