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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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

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Related Experiment Video

Updated: Jun 6, 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

Multisubunit tethering complexes and their role in membrane fusion.

Cornelia Bröcker1, Siegfried Engelbrecht-Vandré, Christian Ungermann

  • 1University of Osnabrück, Department of Biology/Chemistry, Barbarastrasse 13, 49076 Osnabrück, Germany.

Current Biology : CB
|November 9, 2010
PubMed
Summary

Multisubunit tethering complexes are crucial for protein trafficking in eukaryotic cells. These complexes interact with Rab GTPases and SNARE proteins to ensure accurate vesicle fusion within the secretory and endolysosomal pathways.

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A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
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A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

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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

Last Updated: Jun 6, 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

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Organelle Biology

Background:

  • Protein and lipid transport in eukaryotic cells relies on vesicular carriers fusing with organelles.
  • Efficient vesicle capture at organelles involves Rab GTPases and tethering factors.
  • Vesicle fusion is mediated by SNARE proteins, a critical step in intracellular transport.

Purpose of the Study:

  • To review the function of multisubunit tethering complexes in eukaryotic cells.
  • To discuss the role of tethering complexes in the secretory and endolysosomal pathways.
  • To highlight recent findings on tethering complex interactions with Rabs, coat proteins, and SNAREs.

Main Methods:

  • Literature review of current research on protein trafficking and vesicle fusion.
  • Analysis of the mechanisms involving Rab GTPases, tethering complexes, and SNAREs.
  • Focus on the secretory and endolysosomal systems within eukaryotic cells.

Main Results:

  • Multisubunit tethering complexes play a key role in regulating vesicle capture and fusion.
  • These complexes interact with Rab GTPases, influencing their localization and function.
  • Tethering complexes cooperate with SNAREs to ensure efficient and specific vesicle delivery.

Conclusions:

  • Multisubunit tethering complexes are essential regulators of the fusion cascade in eukaryotic cells.
  • Understanding these complexes provides insights into maintaining organelle identity and function.
  • Further research on tethering complexes can reveal new therapeutic targets for diseases related to protein trafficking defects.