Abstract
Tetanus toxin cleaves the synaptic vesicle protein synaptobrevin, and the ensuing loss of neurotransmitter exocytosis has implicated synaptobrevin in this process. To further the study of synaptic function in a genetically tractable organism and to generate a tool to disable neuronal communication for behavioural studies, we have expressed a gene encoding tetanus toxin light chain in Drosophila. Toxin expression in embryonic neurons removes detectable synaptobrevin and eliminates evoked, but not spontaneous, synaptic vesicle release. No other developmental or morphological defects are detected. Correspondingly, only synaptobrevin (n-syb), but not the ubiquitously expressed syb protein, is cleaved by tetanus toxin in vitro. Targeted expression of toxin can produce specific behavioral defects; in one case, the olfactory escape response is reduced.
| Original language | English |
|---|---|
| Pages (from-to) | 341-51 |
| Number of pages | 11 |
| Journal | Neuron |
| Volume | 14 |
| Issue number | 2 |
| Publication status | Published - 1995 |
Keywords
- Amino Acid Sequence
- Animals
- Conserved Sequence
- Drosophila
- Drosophila Proteins
- Embryo, Nonmammalian
- Gene Expression
- Humans
- Immunohistochemistry
- Insect Hormones
- Macromolecular Substances
- Membrane Proteins
- Molecular Sequence Data
- Nerve Tissue Proteins
- Neuromuscular Junction
- Neuropeptides
- R-SNARE Proteins
- Rats
- Recombinant Proteins
- Sequence Homology, Amino Acid
- Synapses
- Synaptic Transmission
- Tetanus Toxin
- Vesicular Transport Proteins