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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...

Coat Assembly and GTPases

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

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.

Rab Proteins

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

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...

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Related Experiment Video

Updated: May 9, 2026

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

GTP-dependent membrane fusion.

James A McNew¹, Holger Sondermann, Tina Lee

¹Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005;

Annual Review of Cell and Developmental Biology

|July 24, 2013

Summary

Membrane remodeling is vital for organelle identity. This review focuses on fusion dynamin-related proteins (DRPs), like atlastin, which are key regulators of endoplasmic reticulum (ER) structure, function, and signaling.

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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

Imaging Plasma Membrane Deformations With pTIRFM

Imaging Plasma Membrane Deformations With pTIRFM

Published on: April 2, 2014

Related Experiment Videos

Last Updated: May 9, 2026

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

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

Imaging Plasma Membrane Deformations With pTIRFM

Imaging Plasma Membrane Deformations With pTIRFM

Published on: April 2, 2014

Area of Science:

Cell Biology
Membrane Biology
Biochemistry

Background:

Membrane dynamics, including shape changes and topological remodeling, are crucial for organelle identity and membrane trafficking.
Organelle membranes possess unique features supporting specialized biological functions, with the endoplasmic reticulum (ER) being a prime example of compartmentalization.
Numerous membrane proteins, including dynamin-related proteins (DRPs), facilitate membrane curvature, fission, and fusion.

Purpose of the Study:

To review recent advancements in the functional and molecular understanding of fusion DRPs.
To highlight the role of atlastin, an ER-resident DRP, in controlling ER structure, function, and signaling.

Main Methods:

Literature review of recent research on fusion DRPs.
Focus on functional and molecular studies of atlastin.

Main Results:

DRPs are key regulators of membrane remodeling.
Atlastin plays a critical role in maintaining ER structure and function.
Fusion DRPs are essential for cellular signaling pathways.

Conclusions:

Fusion DRPs, particularly atlastin, are central to endoplasmic reticulum organization and cellular processes.
Further research into DRPs will illuminate fundamental mechanisms of membrane trafficking and organelle biology.