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

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...
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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.

You might also read

Related Articles

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

Sort by
Same author

LncRNA RUSC1-AS1 promotes the proliferation of hepatocellular carcinoma cells through modulating NOTCH signaling.

Neoplasma·2020
Same author

Predictive Value of Noncontrast Head CT with Negative Findings in the Emergency Department Setting.

AJNR. American journal of neuroradiology·2020
Same author

Self-adjustment and disintegration threshold of Langmuir solitons in inhomogeneous plasmas.

Physical review. E·2017
Same author

Pre-surgical regional blocks in orthognathic surgery: prospective study evaluating their influence on the intraoperative use of anaesthetics and blood pressure control.

International journal of oral and maxillofacial surgery·2016
Same author

Does Ethnic Variability Exist in the Systemic Exposures of OATP1A2 Substrates-Fexofenadine in Taiwanese?

Indian journal of pharmaceutical sciences·2016
Same author

NSD1 mutations generate a genome-wide DNA methylation signature.

Nature communications·2015
Same journal

Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.

Nature reviews. Molecular cell biology·2026
Same journal

How proteins fold.

Nature reviews. Molecular cell biology·2026
Same journal

Single-cell evidence for PANoptosome complexes.

Nature reviews. Molecular cell biology·2026
Same journal

Reply to 'Single-cell evidence for PANoptosome complexes'.

Nature reviews. Molecular cell biology·2026
Same journal

Plucking cellular ribosomes with Ribo-Tweezer.

Nature reviews. Molecular cell biology·2026
Same journal

COPII meets autophagy at the ER membrane.

Nature reviews. Molecular cell biology·2026
See all related articles

Related Experiment Video

Updated: Jun 16, 2026

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

SNARE-mediated membrane fusion.

Y A Chen1, R H Scheller

  • 1Renovis Inc., 747 Fifty Second Street, Oakland, California 94609, USA. yuchen@concentric.net

Nature Reviews. Molecular Cell Biology
|March 17, 2001
PubMed
Summary
This summary is machine-generated.

Soluble NSF attachment protein receptors (SNAREs) mediate intracellular membrane fusion. Research explores how these over 30 proteins ensure transport specificity through their interactions, a mechanism still debated.

More Related Videos

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

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

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

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

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
  • Biochemistry

Background:

  • Soluble NSF attachment protein receptors (SNAREs) are key mediators of intracellular membrane fusion.
  • Over 30 SNARE proteins exist in mammalian cells, each localized to specific subcellular compartments.
  • SNAREs are thought to confer specificity to membrane transport, but the precise mechanism is debated.

Purpose of the Study:

  • To investigate the mechanism by which SNARE proteins achieve membrane transport specificity.
  • To explore the functional interactions between SNARE proteins in driving lipid bilayer fusion.

Main Methods:

  • Functional studies of SNARE protein interactions.
  • Analysis of SNARE protein localization and function in mammalian cells.

Main Results:

  • SNARE proteins are essential for intracellular membrane fusion.
  • Functional studies provide insights into SNARE protein interactions.
  • Evidence suggests SNAREs contribute to membrane transport specificity.

Conclusions:

  • SNARE proteins play a critical role in intracellular membrane fusion and transport specificity.
  • Further research is needed to fully elucidate the controversial mechanisms of SNARE-mediated specificity.