Abstract
Release of neurotransmitter from presynaptic nerve terminals is mediated by SNARE proteins, which are located on the vesicle and plasma membranes. These proteins form a SNARE complex thought to mediate membrane fusion. Complexin is a soluble protein essential for transmitter release, which has been postulated to bind to and stabilise the SNARE complex. We have cloned a complexin homologue, Hm-cpx1, from the leech, Hirudo medicinalis. This protein is expressed in only a subset of neurons in the leech CNS, including the Retzius and P neurons. It is 33% identical to rat complexin I, and 44% identical to squid complexin. Sequence conservation is particularly high in the predicted SNARE binding domain.
| Original language | English |
|---|---|
| Pages (from-to) | 93-7 |
| Number of pages | 5 |
| Journal | Gene Expression Patterns |
| Volume | 4 |
| Issue number | 1 |
| Publication status | Published - Jan 2004 |
Keywords
- Amino Acid Sequence
- Animals
- Central Nervous System
- Cloning, Molecular
- Gene Expression Profiling
- In Situ Hybridization
- Leeches
- Molecular Sequence Data
- Nerve Tissue Proteins
- Phylogeny
- Sequence Homology, Amino Acid