Kalwy S A, Smith R
Department of Biochemistry, University of Queensland, Brisbane, Australia.
Mol Membr Biol. 1994 Apr-Jun;11(2):67-78. doi: 10.3109/09687689409162223.
The segregation of proteins to specific cellular membranes is recognized as a common phenomenon. In oligodendrocytes of the central nervous system, localization of certain proteins to select regions of the plasma membrane gives rise to the myelin membrane. Whilst the fundamental structure and composition of myelin is well understood, less is known of the mechanisms by which the constituent proteins are specifically recruited to those regions of plasma membrane that are forming myelin. The two principal proteins of myelin, the myelin basic protein and proteolipid protein, differ greatly in character and sites of synthesis. The message for myelin basic protein is selectively translocated to the ends of the cell processes, where it is translated on free ribosomes and is incorporated directly into the membrane. Proteolipid protein synthesized at the rough endoplasmic reticulum, processed through the Golgi apparatus, and presumably transported via vesicles to the myelin membrane. This review examines the mechanisms by which these two proteins are targeted to the myelin membrane.
蛋白质向特定细胞膜的分选被认为是一种常见现象。在中枢神经系统的少突胶质细胞中，某些蛋白质定位于质膜的特定区域，从而形成髓鞘膜。虽然髓鞘的基本结构和组成已为人熟知，但对于组成髓鞘的蛋白质如何被特异性招募到正在形成髓鞘的质膜区域的机制，人们了解较少。髓鞘的两种主要蛋白质，即髓鞘碱性蛋白和蛋白脂蛋白，在性质和合成部位上有很大差异。髓鞘碱性蛋白的信使核糖核酸被选择性转运到细胞突起的末端，在那里它在游离核糖体上被翻译，并直接整合到膜中。蛋白脂蛋白在糙面内质网合成，经高尔基体加工，推测通过囊泡运输到髓鞘膜。本综述探讨了这两种蛋白质靶向髓鞘膜的机制。
