Klausner R D
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
New Biol. 1989 Oct;1(1):3-8.
Many integral membrane proteins exist on the plasma membrane as part of multicomponent complexes. In addition to correctly transporting newly synthesized proteins from their site of synthesis in the endoplasmic reticulum to the plasma membrane, the cell must possess mechanisms to ensure that the complexes expressed on the cell surface are accurately assembled. The cell appears to accomplish this feat by superimposing a set of constraints on the newly synthesized membrane proteins whereby the structure and state of assembly of the protein determine its intracellular fate. These processes impose a dramatic level of post-translational regulation on the expression of surface membrane protein complexes. By and large, the cell uses these mechanisms to dispose of, or "edit out," newly synthesized proteins that are not correctly assembled or folded. This review will describe current views of the processes of architectural editing, with an emphasis on the regulation of cell surface expression of the multicomponent T-cell antigen receptor complex.
许多整合膜蛋白作为多组分复合物的一部分存在于质膜上。除了将新合成的蛋白质从内质网中的合成位点正确运输到质膜外，细胞还必须具备确保在细胞表面表达的复合物精确组装的机制。细胞似乎通过对新合成的膜蛋白施加一组限制来实现这一壮举，由此蛋白质的结构和组装状态决定其细胞内命运。这些过程对表面膜蛋白复合物的表达施加了显著水平的翻译后调控。总体而言，细胞利用这些机制来处理或“编辑掉”未正确组装或折叠的新合成蛋白质。本综述将描述目前对结构编辑过程的看法，重点是多组分T细胞抗原受体复合物的细胞表面表达调控。
