Whiteheart S W, Brunner M, Wilson D W, Wiedmann M, Rothman J E
Program of Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, New York 10021.
J Biol Chem. 1992 Jun 15;267(17):12239-43.
Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) are required for the binding of N-ethylmaleimide-sensitive fusion protein (NSF) to Golgi membranes and are, therefore, required for intra-Golgi transport. We report the existence of distinct alpha/beta-SNAP and gamma-SNAP-binding sites in Golgi membranes that appear to be part of the same receptor complex. Cross-linking studies with alpha-SNAP demonstrate that an integral membrane protein of between 30-40 kDa is the alpha-SNAP binding component of the multi-SNAP receptor complex. These data suggest that SNAPs function by independently binding to a multi-SNAP membrane-receptor complex, thereby activating them to serve as adaptors for the targeting of NSF.
可溶性N - 乙基马来酰亚胺敏感融合附着蛋白（SNAPs）是N - 乙基马来酰亚胺敏感融合蛋白（NSF）与高尔基体膜结合所必需的，因此也是高尔基体内部运输所必需的。我们报告在高尔基体膜中存在不同的α/β - SNAP和γ - SNAP结合位点，它们似乎是同一受体复合物的一部分。用α - SNAP进行的交联研究表明，一种30 - 40 kDa的整合膜蛋白是多SNAP受体复合物的α - SNAP结合成分。这些数据表明，SNAPs通过独立结合多SNAP膜受体复合物发挥作用，从而激活它们作为NSF靶向的衔接子。
