Guan J L, Rose J K
Cell. 1984 Jul;37(3):779-87. doi: 10.1016/0092-8674(84)90413-6.
We have carried out experiments designed to ask if it is possible to convert a secretory protein into an integral membrane protein by appending the membrane spanning domain of an integral membrane protein to its carboxy terminus. We first obtained expression of a cDNA clone encoding rat growth hormone (rGH) in eucaryotic cells, and found that this protein was secreted. We then constructed and expressed a hybrid gene encoding rGH fused to the membrane spanning and cytoplasmic domains of the vesicular stomatitis virus (VSV) glycoprotein (G). This fusion protein was anchored in microsomal membranes in the expected transmembrane configuration. The fusion protein was transported to the Golgi apparatus, and was esterified to palmitic acid, but it was not transported to the cell surface. We suggest that the sorting signal which allows rapid secretion of soluble rGH does not function when the protein is bound to the membrane.
我们进行了一些实验，旨在探究通过将整合膜蛋白的跨膜结构域附加到分泌蛋白的羧基末端，是否有可能将其转化为整合膜蛋白。我们首先在真核细胞中获得了编码大鼠生长激素（rGH）的cDNA克隆的表达，并发现该蛋白是分泌型的。然后我们构建并表达了一个杂交基因，该基因编码与水泡性口炎病毒（VSV）糖蛋白（G）的跨膜和胞质结构域融合的rGH。这种融合蛋白以预期的跨膜构型锚定在微粒体膜中。融合蛋白被转运到高尔基体，并被棕榈酸酯化，但它没有被转运到细胞表面。我们认为，当该蛋白与膜结合时，允许可溶性rGH快速分泌的分选信号不起作用。
