分泌囊泡将酵母中的主要质膜ATP酶运输至细胞外。
Secretory vesicles externalize the major plasma membrane ATPase in yeast.
作者信息
Holcomb C L, Hansen W J, Etcheverry T, Schekman R
机构信息
Department of Biochemistry, University of California, Berkeley 94720.
出版信息
J Cell Biol. 1988 Mar;106(3):641-8. doi: 10.1083/jcb.106.3.641.
Abstract
Yeast cell surface growth is accomplished by constitutive secretion and plasma membrane assembly, culminating in the fusion of vesicles with the bud membrane. Coordination of secretion and membrane assembly has been investigated by examining the biogenesis of plasma membrane ATPase (PM ATPase) in secretion-defective (sec) strains of Saccharomyces cerevisiae. PM ATPase is synthesized as a approximately 106-kD polypeptide that is not detectably modified by asparagine-linked glycosylation or proteolysis during transit to the plasma membrane. Export of the PM ATPase requires the secretory pathway. In sec1, a mutant defective in the last step of secretion, large amounts of Golgi-derived vesicles are accumulated. Biochemical characterization of this organelle has demonstrated that PM ATPase and the secretory enzyme, acid phosphatase, are transported in a single vesicle species.
摘要
酵母细胞表面生长通过组成型分泌和质膜组装来完成，最终导致囊泡与芽膜融合。通过研究酿酒酵母分泌缺陷型（sec）菌株中质膜ATP酶（PM ATP酶）的生物发生，对分泌和膜组装的协调进行了研究。PM ATP酶作为一种约106-kD的多肽合成，在转运到质膜的过程中，未检测到其被天冬酰胺连接的糖基化或蛋白水解修饰。PM ATP酶的输出需要分泌途径。在sec1中，一种在分泌最后一步有缺陷的突变体，积累了大量来自高尔基体的囊泡。对该细胞器的生化特性分析表明，PM ATP酶和分泌酶酸性磷酸酶在单一囊泡种类中运输。
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