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

11.0K
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...
11.0K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

11.2K
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...
11.2K
Rab Cascades01:25

Rab Cascades

2.7K
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.
2.7K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.6K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
2.6K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.8K
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,...
5.8K

You might also read

Related Articles

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

Sort by
Same author

Molecular insight into microtubule nucleation by the XMAP215/γ-TuRC module.

Nature communications·2026
Same author

Structural insights into xyloglucan recognition by an ABC transporter from a Gram-positive, thermophilic bacterium.

bioRxiv : the preprint server for biology·2025
Same author

Engineering auxin degradation into root-associated bacteria promotes plant growth.

bioRxiv : the preprint server for biology·2025
Same author

How augmin establishes the angle of the microtubule branch site.

Nature communications·2025
Same author

Discovery of a widespread chemical signalling pathway in the Bacteroidota.

Nature·2025
Same author

Functional and structural characterization of AtAbf43C: an exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313.

The Biochemical journal·2025

Related Experiment Video

Updated: Aug 10, 2025

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

10.9K

Structure of a Membrane Tethering Complex Incorporating Multiple SNAREs.

Kevin A DAmico1, Abigail E Stanton1, Jaden D Shirkey1

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ 08544.

Biorxiv : the Preprint Server for Biology
|February 13, 2023
PubMed
Summary

The Dsl1 complex, a membrane tethering complex, binds to SNAREs and reveals common principles of MTC function, suggesting tethers and SNAREs work as one machine.

More Related Videos

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

9.7K
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

14.1K

Related Experiment Videos

Last Updated: Aug 10, 2025

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

10.9K
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

9.7K
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

14.1K

Area of Science:

  • Cellular biology
  • Structural biology

Background:

  • Membrane fusion in eukaryotic cells relies on membrane tethering complexes (MTCs) and SNARE proteins.
  • MTCs initiate membrane attachment, while SNAREs bridge membranes for fusion.

Approach:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of the Dsl1 complex bound to endoplasmic reticulum-anchoring SNAREs.
  • Comparative analysis with the exocyst MTC was performed.

Key Points:

  • The 255-kDa Dsl1 complex structure reveals SNARE N-terminal domains integral to the complex.
  • The Dsl1 complex configuration shows unexpected similarities to the 850-kDa exocyst MTC.
  • This suggests conserved mechanisms for MTC function.

Conclusions:

  • Common principles of MTC function are likely shared across different complexes.
  • Tethers and SNAREs may function collaboratively as an integrated machine in membrane fusion.