Morgan A, Burgoyne R D
Physiological Laboratory, University of Liverpool, PO Box 147, L69 3BX, Liverpool, UK.
Trends Cell Biol. 1995 Sep;5(9):335-9. doi: 10.1016/s0962-8924(00)89059-5.
N-ethylmaleimide-sensitive fusion protein (NSF) is an ATPase required for vesicular transport throughout the constitutive secretory and endocytic pathways. Recently, NSF has also been implicated in regulated exocytosis in synapses--based on SNAP-mediated binding in vitro to a complex of neurotoxin substrates (termed 'SNAREs'). This work has generated an hypothesis in which the interaction of SNAREs (SNAP receptors) on the vesicle membrane with those on the target membrane forms a docking complex to which SNAPs bind, thus allowing NSF to bind and elicit membrane fusion. However, current evidence supports an earlier, pre-fusion role for NSF. We speculate that this role may be as a molecular chaperone for the membrane docking/fusion machinery.
N - 乙基马来酰亚胺敏感融合蛋白(NSF)是一种ATP酶,在整个组成型分泌和内吞途径的囊泡运输中发挥作用。最近,基于体外SNAP介导的与神经毒素底物复合物(称为“SNAREs”)的结合,NSF也被认为参与了突触中的调节性胞吐作用。这项研究提出了一个假说,即囊泡膜上的SNAREs(SNAP受体)与靶膜上的SNAREs相互作用形成一个对接复合物,SNAP与之结合,从而使NSF能够结合并引发膜融合。然而,目前的证据支持NSF在融合前发挥更早的作用。我们推测这个作用可能是作为膜对接/融合机制的分子伴侣。