Gillingham Alison K, Munro Sean
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
Biochim Biophys Acta. 2003 Aug 18;1641(2-3):71-85. doi: 10.1016/s0167-4889(03)00088-0.
Protein transport between organelles is mediated by vesicles which must accurately dock and fuse with appropriate compartments. Over the past several years a large number of long coiled-coil proteins have been identified on the Golgi and on endosomes, mostly as auto-antigens in autoimmune disorders. Based on their restricted intracellular distributions and their predicted rod-like structure, these proteins have been proposed to play a role in tethering vesicles to target organelles prior to fusion. However, such proteins may also play a structural role, for example as components of a Golgi matrix, or as scaffolds for the assembly of other factors important for fusion. This review will examine what is known about the function of these large coiled-coil proteins in membrane traffic.
细胞器之间的蛋白质运输由囊泡介导，囊泡必须准确对接并与适当的区室融合。在过去几年中，在高尔基体和内体上发现了大量长卷曲螺旋蛋白，其中大多数是自身免疫性疾病中的自身抗原。基于它们在细胞内的有限分布以及预测的棒状结构，这些蛋白被认为在囊泡与靶细胞器融合之前将囊泡拴系到靶细胞器上发挥作用。然而，这类蛋白也可能发挥结构作用，例如作为高尔基体基质的成分，或作为对融合重要的其他因子组装的支架。本综述将探讨关于这些大型卷曲螺旋蛋白在膜运输中的功能的已知信息。
