Okita Thomas W., Rogers John C.
Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340, Department of Biochemistry, University of Missouri, Columbia, Missouri 65211.
Annu Rev Plant Physiol Plant Mol Biol. 1996 Jun;47:327-350. doi: 10.1146/annurev.arplant.47.1.327.
This review focuses on four interrelated processes in the plant endomembrane system: compartmentation of proteins in subdomains of the endoplasmic reticulum, mechanisms that determine whether storage proteins are retained within the ER lumen or transported out, the origin and function of biochemically distinct vacuoles or prevacuolar organelles, and the cellular processes by which proteins are sorted to vacuolar compartments. We postulate that ER-localized protein bodies are formed by a series of orderly events of protein synthesis, protein concentration, and protein assembly in subdomains of the ER. Protein concentration, which facilitates protein-to-protein interactions and subsequent protein assembly, may be achieved by the interactions with chaperones and by the localization of storage protein mRNAs. We also describe recent developments on the coexistence of two biochemically distinguishable vacuolar compartments, the possible direct role of the ER in vacuole biogenesis, and proposed mechanisms for transport of proteins from the ER or Golgi apparatus to the vacuole.
内质网亚结构域中蛋白质的区室化、决定储存蛋白是保留在内质网腔还是转运出去的机制、生化特性不同的液泡或前液泡细胞器的起源和功能，以及蛋白质被分选到液泡区室的细胞过程。我们推测，内质网定位的蛋白体是由内质网亚结构域中一系列有序的蛋白质合成、蛋白质浓缩和蛋白质组装事件形成的。蛋白质浓缩促进了蛋白质与蛋白质之间的相互作用以及随后的蛋白质组装，这可能通过与伴侣蛋白的相互作用以及储存蛋白mRNA 的定位来实现。我们还描述了关于两种生化特性可区分的液泡区室共存的最新进展、内质网在液泡生物发生中可能的直接作用，以及从内质网或高尔基体向液泡转运蛋白质的推测机制。
