Related Experiment Video
Updated: Dec 15, 2025

09:33
An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
Published on: June 26, 2018
7.8K
The diversity of synaptotagmin isoforms
1Department of Brain Sciences, Division of Neuroscience, Imperial College London, Hammersmith Hospital Campus, Du Cane Road, London, W12 0NN, UK; UK Dementia Research Institute at Imperial College, London, UK.
Current Opinion in Neurobiology
|July 15, 2020
Summary
Synaptotagmins regulate calcium-dependent membrane fusion. This review explores all 17 synaptotagmin isoforms, revealing diverse roles beyond neurotransmitter release in brain function.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Synaptotagmin family regulates calcium-dependent membrane fusion.
- 17 synaptotagmin isoforms exist in mice and humans.
- Focus has been on isoforms 1, 2, and 7 for synaptic vesicle exocytosis.
Purpose of the Study:
- Highlight the diversity of synaptotagmins.
- Summarize key findings on all isoforms.
- Discuss different ways of grouping synaptotagmin isoforms.
Main Methods:
- Literature review of synaptotagmin research.
- Analysis of studies on all 17 synaptotagmin isoforms.
- Synthesis of findings on isoform function, localization, and interactions.
Main Results:
- Synaptotagmins have diverse roles beyond neurotransmitter release, including receptor endocytosis, vesicle trafficking, membrane repair, synaptic plasticity, and neuroprotection.
- Isoforms function in neurons and glia, at various developmental timepoints.
- Synaptotagmins exhibit complex expression patterns, including splice variants, homo- and heterodimers, and varied subcellular localization.
Conclusions:
- The synaptotagmin family is more diverse than previously appreciated.
- Understanding all isoforms is crucial for comprehending brain function.
- Further research into synaptotagmin diversity will uncover new therapeutic targets.
Related Concept Videos
SNAREs and Membrane Fusion
12.1K
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...
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...
12.1K
Overview of Myosin Structure and Function
5.8K
Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X) have been well...
5.8K
Introduction to Actin
6.1K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across...
6.1K

