The worm SNARE complex and it's regulators for vesicle neurotransmetter and neuropeptide release (Gracheva et al. 2007). The SNARE complex consists of Syntaxin, SNAP and Synaptobrevin and mediates the synaptic vesicle cycle (Rathore et al. 2010). Synaptotagmin I is a Ca2+ sensor triggering vesicle fusion (Yu et al. 2013). Regulators include Snapin dimers (Yu et al. 2013), Complexin, a presynaptic protein that interacts with the SNARE complex; the C-terminal domain binds lipids to inhibit exocytosis (Hobson et al. 2011; Wragg et al. 2013), Unc-18, which binds syntaxin and regluates synaptic vesicle (neurotransmitter) docking (Graham et al. 2011), Unc13 which also regluates docking of the synaptic vescicles to the plasma membrane by interacting with syntaxin, CAPS or Unc31, a Ca2+-activated protein for secretion that is required for dense core vesicle docking for neuropeptide release (Lin et al. 2010), and Tomosyn or Tom-1, a negative regluator of both neurotransmitter and neuropeptide release (Gracheva et al. 2007).
|Protein Name:||SNAPIN protein homolog|
|Species:||Caenorhabditis elegans  |
1: MSSTAGGEVS INSGDLLLGT LSTSITKLEQ QIRATQLSQK KLNSDCETMA EYLRDLSEYK
61: QPVDLLPYVG KLNDSTIRVN NTHQKLDDLL ERLTKLQRQI ARETYKKKNS IKEQEPPVQP