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SNAREs and Membrane Fusion

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 Membrane

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 Cascades

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.

Vesicular Tubular Clusters

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...

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

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...

Assembly of Signaling Complexes

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,...

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Related Experiment Video

Updated: Jul 6, 2025

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

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

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, USA.

Nature Structural & Molecular Biology

|January 10, 2024

Summary

The study reveals the structure of the Dsl1 complex tethering complex bound to SNARE proteins, uncovering common principles in membrane fusion. This structure suggests tethers and SNAREs function as an integrated machine.

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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

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

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

Published on: October 19, 2012

Related Experiment Videos

Last Updated: Jul 6, 2025

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

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

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

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

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

Published on: October 19, 2012

Area of Science:

Cell biology
Structural biology
Biochemistry

Background:

Membrane fusion in eukaryotic cells relies on multisubunit tethering complexes (MTCs) and SNARE proteins.
MTCs mediate initial membrane attachment, while SNAREs drive membrane merging.

Purpose of the Study:

To determine the cryo-electron microscopy structure of the Dsl1 complex, the simplest known MTC.
To investigate the interaction between the Dsl1 complex and its cognate SNAREs.

Main Methods:

Cryo-electron microscopy (cryo-EM) was used to determine the structure.
Structural comparison between the Dsl1 complex and the exocyst MTC.

Main Results:

The structure of the 255-kDa Dsl1 complex bound to endoplasmic reticulum-anchoring SNAREs was determined.
Unexpected structural similarities were found between the SNARE-bound Dsl1 complex and the larger exocyst MTC.
SNARE N-terminal domains are integral to the Dsl1 complex structure, stabilizing its conformation.

Conclusions:

The findings suggest common functional principles for MTCs, regardless of size.
Tethering complexes and SNAREs may operate as a unified machine in membrane fusion.