Spear E, Ng D T
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Traffic. 2001 Aug;2(8):515-23. doi: 10.1034/j.1600-0854.2001.20801.x.
The endoplasmic reticulum stress pathway known as the unfolded protein response is currently the best understood model of interorganellar signal transduction. Bridging a physical separation, the pathway provides a direct line of communication between the endoplasmic reticulum lumen and the nucleus. With the unfolded protein response, the cell has the means to monitor and respond to the changing needs of the endoplasmic reticulum. Beginning with the discovery of its remarkable signaling mechanism in yeast, the unfolded protein response has not ceased to reveal more of its many secrets. By applying powerful biochemical, genetic, genomic, and cytological approaches, the recent efforts of many groups have buried the long-held notion that the unfolded protein response is simply a regulatory platform for endoplasmic reticulum chaperones. We now know that the unfolded protein response regulates many genes that affect diverse aspects of cellular physiology. In addition, studies in mammals have revealed novel unfolded protein response signaling factors that may contribute to the specialized needs of multicellular organisms. This article focuses on these and other recent developments in the field.
被称为未折叠蛋白反应的内质网应激途径是目前细胞内膜间信号转导中理解最为透彻的模型。该途径跨越了物理上的分隔，在内质网腔和细胞核之间提供了一条直接的通讯线路。通过未折叠蛋白反应，细胞能够监测并响应内质网不断变化的需求。自其在酵母中显著的信号传导机制被发现以来，未折叠蛋白反应不断揭示出更多秘密。通过运用强大的生化、遗传、基因组学和细胞学方法，许多研究团队的最新努力打破了长期以来认为未折叠蛋白反应仅仅是内质网伴侣蛋白调节平台的观念。我们现在知道，未折叠蛋白反应调控着许多影响细胞生理多个方面的基因。此外，在哺乳动物中的研究揭示了可能有助于多细胞生物特殊需求的新型未折叠蛋白反应信号因子。本文重点关注该领域的这些及其他最新进展。
