Ma D, Zerangue N, Lin Y F, Collins A, Yu M, Jan Y N, Jan L Y
Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143-0725, USA.
Science. 2001 Jan 12;291(5502):316-9. doi: 10.1126/science.291.5502.316.
Little is known about the identity of endoplasmic reticulum (ER) export signals and how they are used to regulate the number of proteins on the cell surface. Here, we describe two ER export signals that profoundly altered the steady-state distribution of potassium channels and were required for channel localization to the plasma membrane. When transferred to other potassium channels or a G protein-coupled receptor, these ER export signals increased the number of functional proteins on the cell surface. Thus, ER export of membrane proteins is not necessarily limited by folding or assembly, but may be under the control of specific export signals.
内质网（ER）输出信号的特性以及它们如何用于调节细胞表面蛋白质的数量，目前所知甚少。在这里，我们描述了两种内质网输出信号，它们深刻地改变了钾通道的稳态分布，并且是通道定位于质膜所必需的。当转移到其他钾通道或G蛋白偶联受体时，这些内质网输出信号增加了细胞表面功能性蛋白质的数量。因此，膜蛋白的内质网输出不一定受折叠或组装的限制，而可能受特定输出信号的控制。
