Whiteheart S W, Schraw T, Matveeva E A
Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington 40536, USA.
Int Rev Cytol. 2001;207:71-112. doi: 10.1016/s0074-7696(01)07003-6.
Our understanding of the molecular mechanisms of membrane trafficking advanced at a rapid rate during the 1990s. As one of the initial protein components of the trafficking machinery to be identified, N-ethylmaleimide sensitive factor (NSF) has served as a reference point in many of these recent studies. This hexameric ATPase is essential for most of the membrane-trafficking events in a cell. Initially, due to its ATPase activity, NSF was thought to be the motor that drove membrane fusion. Subsequent studies have shown that NSF actually plays the role of a chaperone by activating SNAP receptor proteins (SNAREs) so that they can participate in membrane fusion. In this review we will examine the initial characterization of NSF, its role in membrane fusion events, and what new structural information can tell us about NSF's mechanism of action.
在20世纪90年代，我们对膜运输分子机制的理解迅速发展。作为最早被鉴定的运输机制蛋白质成分之一，N - 乙基马来酰亚胺敏感因子（NSF）在许多近期研究中都作为一个参考点。这种六聚体ATP酶对细胞中的大多数膜运输事件至关重要。最初，由于其ATP酶活性，NSF被认为是驱动膜融合的动力。随后的研究表明，NSF实际上通过激活SNAP受体蛋白（SNARE）发挥伴侣蛋白的作用，从而使它们能够参与膜融合。在这篇综述中，我们将研究NSF的最初特征、它在膜融合事件中的作用，以及新的结构信息能告诉我们关于NSF作用机制的哪些内容。
