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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...

SNAREs and Membrane Fusion

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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.
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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...

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Vesicular Tubular Clusters

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Related Experiment Video

Updated: Jun 11, 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

SNARE conformational changes that prepare vesicles for exocytosis.

Noriko Takahashi¹, Hiroyasu Hatakeyama, Haruo Okado

¹Laboratory of Structural Physiology, Center for Disease Biology and Integrative Medicine, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan. norikomd@m.u-tokyo.ac.jp

Cell Metabolism

|July 13, 2010

Summary

SNARE proteins, crucial for exocytosis, exist in preassembled states enabling rapid hormone release. Calcium influx can also trigger slower SNARE assembly and subsequent slower exocytosis in beta cells.

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

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Area of Science:

Cell Biology
Neuroscience
Endocrinology

Background:

Exocytosis is a fundamental cellular process for releasing hormones and neurotransmitters.
Cytosolic calcium (Ca2+) influx triggers vesicle fusion with the plasma membrane.
SNARE protein complex assembly is known to be essential for this membrane fusion event.

Purpose of the Study:

To investigate the precise timing of SNARE complex assembly relative to vesicle fusion during exocytosis.
To understand how SNARE protein configurations influence the kinetics of exocytosis.

Main Methods:

Development of a Förster Resonance Energy Transfer (FRET) based probe to detect SNAP25 and syntaxin-1A plasma membrane SNARE complex assembly.
Simultaneous measurement of FRET signals and insulin exocytosis using two-photon imaging in pancreatic beta cells.

Main Results:

Demonstrated that SNARE complex assembly can be preassembled in certain cellular regions, facilitating rapid exocytosis.
Observed that in other regions, SNARE assembly occurs after calcium (Ca2+) influx, leading to slower exocytosis.
Revealed distinct SNARE protein configurations influencing exocytosis kinetics.

Conclusions:

SNARE proteins exist in multiple stable, preparatory configurations prior to calcium influx.
Calcium (Ca2+) can trigger exocytosis through distinct mechanisms depending on SNARE complex status.
This finding provides crucial insights into the regulation and variability of exocytosis kinetics.