Cloning and expression of a leech complexin.
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.
Dykes
Iain M
IM
Division of Biology, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0368, USA.
Davies
Jane A
JA
D000595:Amino Acid Sequence; D000818:Animals; D002490:Central Nervous System / Q000378:metabolism; D003001:Cloning, Molecular; D020869:Gene Expression Profiling; D017403:In Situ Hybridization; D007865:Leeches / Q000235:genetics*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000235:genetics*; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
D009419:Nerve Tissue Proteins