Thomas L, Hartung K, Langosch D, Rehm H, Bamberg E, Franke W W, Betz H
Zentrum für Molekulare Biologie, Universität Heidelberg, Federal Republic of Germany.
Science. 1988 Nov 18;242(4881):1050-3. doi: 10.1126/science.2461586.
The quaternary structure and functional properties of synaptophysin, a major integral membrane protein of small presynaptic vesicles, were investigated. Cross-linking and sedimentation studies indicate that synaptophysin is a hexameric homo-oligomer, which in electron micrographs exhibits structural features common to channel-forming proteins. On reconstitution into planar lipid bilayers, purified synaptophysin displays voltage-sensitive channel activity with an average conductance of about 150 picosiemens. Because specific channels and fusion pores have been implicated in vesicular uptake and release of secretory compounds, synaptophysin may have a role in these processes.
研究了突触囊泡蛋白（小突触前囊泡的一种主要整合膜蛋白）的四级结构和功能特性。交联和沉降研究表明，突触囊泡蛋白是一种六聚体同型寡聚体，在电子显微镜下呈现出通道形成蛋白共有的结构特征。在重组到平面脂质双分子层中时，纯化的突触囊泡蛋白表现出电压敏感通道活性，平均电导率约为150皮西门子。由于特定通道和融合孔与分泌性化合物的囊泡摄取和释放有关，突触囊泡蛋白可能在这些过程中发挥作用。
