Chin A C, Burgess R W, Wong B R, Schwarz T L, Scheller R H
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305-5428.
Gene. 1993 Sep 15;131(2):175-81. doi: 10.1016/0378-1119(93)90291-a.
VAMP (synaptobrevin) is a highly conserved membrane protein originally described as a component of brain synaptic vesicles. The Drosophila melanogaster VAMP-encoding gene (syb) comprises five exons. Splicing exons 1,2,3,4,5 (syb-b) results in a protein with a C-terminal hydrophobic domain and a negligible intraluminal domain. Splicing exons 1,2,3,5 (syb-a) predicts a protein with a 20-amino-acid luminal domain at the C terminus. The ratio of syb-a to syb-b transcripts is highly regulated during development. The syb transcripts show no enrichment in the nervous system and are present in very early embryos, well before neurogenesis. The greatest concentration of syb transcripts was found in cells of the gut and malpighian tubules. Thus, syb may have a general role in membrane trafficking and, perhaps, a role in the secretion of digestive enzymes.
VAMP（突触小泡蛋白）是一种高度保守的膜蛋白，最初被描述为脑突触小泡的一个组成部分。果蝇的VAMP编码基因（syb）由五个外显子组成。剪接外显子1、2、3、4、5（syb-b）产生一种具有C末端疏水结构域和可忽略不计的腔内结构域的蛋白质。剪接外显子1、2、3、5（syb-a）预测一种在C末端具有20个氨基酸腔内结构域的蛋白质。在发育过程中，syb-a与syb-b转录本的比例受到高度调控。syb转录本在神经系统中没有富集，并且在神经发生很早之前的非常早期胚胎中就存在。syb转录本的最高浓度出现在肠道和马氏管的细胞中。因此，syb可能在膜运输中具有一般作用，也许在消化酶的分泌中也有作用。
