UNC-13L, UNC-13S, and Tomosyn form a protein code for fast and slow neurotransmitter release in Caenorhabditis elegans

Synaptic transmission consists of fast and slow components of neurotransmitter release. Here we show that these components are mediated by distinct exocytic proteins. The Caenorhabditis elegans unc-13 gene is required for SV exocytosis, and encodes long and short isoforms (UNC-13L and S). Fast relea...

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Bibliographic Details
Published in:eLife 2013-08, Vol.2, p.e00967-e00967
Main Authors: Hu, Zhitao, Tong, Xia-Jing, Kaplan, Joshua M
Format: Article
Language:English
Subjects:
Acetylcholine - metabolism
Animals
Caenorhabditis elegans
Caenorhabditis elegans - genetics
Caenorhabditis elegans - metabolism
Caenorhabditis elegans Proteins - genetics
Caenorhabditis elegans Proteins - metabolism
Calcium channels
Calcium-binding protein
Calmodulin
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Biology
Exocytosis
Isoforms
Kinetics
Latency
Localization
Munc13
Nematodes
Neuroscience
Neurosciences
Neurotransmitter release
Protein Isoforms - genetics
Protein Isoforms - metabolism
Proteins
Rats
Sensors
Spatial discrimination
Subcellular Fractions - metabolism
Synapses - physiology
Synaptic transmission
TOM-1
Tomosyn
UNC-13
Young adults
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Summary:Synaptic transmission consists of fast and slow components of neurotransmitter release. Here we show that these components are mediated by distinct exocytic proteins. The Caenorhabditis elegans unc-13 gene is required for SV exocytosis, and encodes long and short isoforms (UNC-13L and S). Fast release was mediated by UNC-13L, whereas slow release required both UNC-13 proteins and was inhibited by Tomosyn. The spatial location of each protein correlated with its effect. Proteins adjacent to the dense projection mediated fast release, while those controlling slow release were more distal or diffuse. Two UNC-13L domains accelerated release. C2A, which binds RIM (a protein associated with calcium channels), anchored UNC-13 at active zones and shortened the latency of release. A calmodulin binding site accelerated release but had little effect on UNC-13's spatial localization. These results suggest that UNC-13L, UNC-13S, and Tomosyn form a molecular code that dictates the timing of neurotransmitter release. DOI:http://dx.doi.org/10.7554/eLife.00967.001.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.00967