Grote E, Carr C M, Novick P J
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
J Cell Biol. 2000 Oct 16;151(2):439-52. doi: 10.1083/jcb.151.2.439.
In yeast, assembly of exocytic soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor (SNARE) complexes between the secretory vesicle SNARE Sncp and the plasma membrane SNAREs Ssop and Sec9p occurs at a late stage of the exocytic reaction. Mutations that block either secretory vesicle delivery or tethering prevent SNARE complex assembly and the localization of Sec1p, a SNARE complex binding protein, to sites of secretion. By contrast, wild-type levels of SNARE complexes persist in the sec1-1 mutant after a secretory block is imposed, suggesting a role for Sec1p after SNARE complex assembly. In the sec18-1 mutant, cis-SNARE complexes containing surface-accessible Sncp accumulate in the plasma membrane. Thus, one function of Sec18p is to disassemble SNARE complexes on the postfusion membrane.
在酵母中，分泌囊泡SNARE蛋白Sncp与质膜SNARE蛋白Ssop和Sec9p之间的外排可溶性N - 乙基马来酰亚胺敏感融合蛋白（NSF）附着蛋白受体（SNARE）复合物的组装发生在外排反应的后期。阻断分泌囊泡运输或拴系的突变会阻止SNARE复合物的组装以及SNARE复合物结合蛋白Sec1p在分泌位点的定位。相比之下，在施加分泌阻断后，sec1 - 1突变体中SNARE复合物的野生型水平持续存在，这表明Sec1p在SNARE复合物组装后发挥作用。在sec18 - 1突变体中，含有可接近表面的Sncp的顺式SNARE复合物在质膜中积累。因此，Sec18p的一个功能是拆解融合后膜上的SNARE复合物。
