Frand A R, Cuozzo J W, Kaiser C A
Dept of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Trends Cell Biol. 2000 May;10(5):203-10. doi: 10.1016/s0962-8924(00)01745-1.
The folding of many secretory proteins depends upon the formation of disulphide bonds. Recent advances in genetics and cell biology have outlined a core pathway for disulphide bond formation in the endoplasmic reticulum (ER) of eukaryotic cells. In this pathway, oxidizing equivalents flow from the recently identified ER membrane protein Ero1p to secretory proteins via protein disulphide isomerase (PDI). Contrary to prior expectations, oxidation of glutathione in the ER competes with oxidation of protein thiols. Contributions of PDI homologues to the catalysis of oxidative folding will be discussed, as will similarities between eukaryotic and prokaryotic disulphide-bond-forming systems.
许多分泌蛋白的折叠依赖于二硫键的形成。遗传学和细胞生物学的最新进展勾勒出了真核细胞内质网（ER）中二硫键形成的核心途径。在该途径中，氧化当量从最近鉴定出的内质网膜蛋白Ero1p通过蛋白质二硫键异构酶（PDI）流向分泌蛋白。与先前的预期相反，内质网中谷胱甘肽的氧化与蛋白质巯基的氧化相互竞争。将讨论PDI同源物对氧化折叠催化的贡献，以及真核和原核二硫键形成系统之间的相似性。
