Ungermann C, Sato K, Wickner W
Dartmouth Medical School, Department of Biochemistry, Hanover, New Hampshire 03755, USA.
Nature. 1998 Dec 10;396(6711):543-8. doi: 10.1038/25069.
The homotypic fusion of yeast vacuoles includes a 'docking' step, which we show here to consist of two sequential reactions: a reversible 'tethering' mediated by the GTPase Ypt7, and 'SNARE pairing', in which SNARE proteins from opposite membranes form a complex in trans. The function of this trans-SNARE complex must be transient, as the complex can be disassembled by excess Sec18 in the presence of Sec17 and ATP without influencing the fusion rate. These data indicate that SNARE pairing may transiently signal to downstream factors, leading to fusion.
酵母液泡的同型融合包括一个“对接”步骤，我们在此表明该步骤由两个连续反应组成：由GTP酶Ypt7介导的可逆“拴系”，以及“SNARE配对”，即来自相对膜的SNARE蛋白在反式中形成复合物。这种反式SNARE复合物的功能必须是短暂的，因为在Sec17和ATP存在的情况下，过量的Sec18可以将该复合物拆解，而不影响融合速率。这些数据表明，SNARE配对可能会短暂地向下游因子发出信号，从而导致融合。
