内质网衍生的运输小泡与纯化的酵母高尔基体膜靶向融合的生化要求。
Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes.
作者信息
Lupashin V V, Hamamoto S, Schekman R W
机构信息
Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
出版信息
J Cell Biol. 1996 Feb;132(3):277-89. doi: 10.1083/jcb.132.3.277.
Abstract
In order for secretion to progress, ER-derived transport vesicles must target to, and fuse with the cis-Golgi compartment. These processes have been reconstituted using highly enriched membrane fractions and partially purified soluble components. The functionally active yeast Golgi membranes that have been purified are highly enriched in the cis-Golgi marker enzymes alpha 1,6 mannosyltransferase and GDPase. Fusion of transport vesicles with these membranes requires both GTP and ATP hydrolysis, and depends on cytosolic and peripheral membrane proteins. At least two protein fractions from yeast cytosol are required for the reconstitution of ER-derived vesicle fusion. Soluble fractions prepared from temperature-sensitive mutants revealed requirements for the Ypt1p, Sec19p, Sly1p, Sec7p, and Uso1 proteins. A model for the sequential involvement of these components in the targeting and fusion reaction is proposed.
摘要
为了使分泌过程顺利进行，源自内质网的运输小泡必须靶向顺式高尔基体区室并与之融合。这些过程已使用高度富集的膜组分和部分纯化的可溶性成分进行了重建。已纯化的具有功能活性的酵母高尔基体膜富含顺式高尔基体标记酶α1,6甘露糖基转移酶和GDP酶。运输小泡与这些膜的融合既需要GTP水解也需要ATP水解，并且依赖于胞质和外周膜蛋白。内质网衍生小泡融合的重建至少需要来自酵母胞质溶胶的两种蛋白质组分。从温度敏感突变体制备的可溶性组分揭示了对Ypt1p、Sec19p、Sly1p、Sec7p和Uso1蛋白的需求。提出了这些组分在靶向和融合反应中顺序参与的模型。
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