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Related Experiment Video

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Single-Cell Calcium Imaging for Studying the Activation of Calcium Ion Channels

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Published on: December 13, 2024

Calcium sensitive ring-like oligomers formed by synaptotagmin.

Jing Wang¹, Oscar Bello¹, Sarah M Auclair¹

¹Departments of Cell Biology.

Proceedings of the National Academy of Sciences of the United States of America

|September 10, 2014

Summary

Synaptotagmin-1 (SYT) forms rings on membranes without calcium, acting as a clamp. Calcium disrupts these rings, enabling neurotransmitter release by allowing SNARE complex assembly.

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Area of Science:

Molecular Biology
Neuroscience
Structural Biology

Background:

Synaptotagmin-1 (SYT) is crucial for calcium-dependent neurotransmitter release.
The precise structural mechanism of SYT's role in membrane fusion remains elusive.

Purpose of the Study:

To elucidate the structural mechanism of synaptotagmin-1 in membrane fusion.
To investigate the role of SYT's cytosolic domain (C2AB) in protein-lipid interactions.

Main Methods:

Electron microscopy was used to visualize SYT structures on lipid monolayers.
Helical reconstruction was employed to determine the structure of SYT tubes.
The effect of calcium and magnesium ions on SYT ring formation was assessed.

Main Results:

An unexpected circular arrangement (ring) of SYT's C2AB domain was observed in the absence of calcium.
These SYT rings, composed of 11-26 molecules, can stack to form protein-coated tubes.
Calcium ions rapidly disrupt the SYT rings, while magnesium ions do not.

Conclusions:

SYT rings may act as a clamp, preventing SNARE complex assembly and thus inhibiting fusion in the absence of calcium.
Calcium-induced disassembly of SYT rings facilitates neurotransmitter release by allowing fusion to proceed.