School of Molecular and Systems Medicine, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada.
Arch Biochem Biophys. 2011 Jun 1;510(1):1-10. doi: 10.1016/j.abb.2011.03.010. Epub 2011 Mar 31.
Many membrane proteins are functional as stable oligomers. An understanding of the conditions that elicit and enhance oligomerization is important in many therapeutics. In this regard, protein-protein and protein-lipid interactions play crucial roles in the assembly and stability of oligomeric complexes. Recent years have seen a rapid increase in the mechanistic information on the importance of cytoplasmic termini in determining subunit assembly and stability of oligomeric complexes. In addition, the role of specific protein-lipid interaction between anionic phospholipids and "hot spots" on the protein surface has also become evident in stabilizing oligomeric assemblies. This review focuses on several contemporary developments of membrane proteins that stabilize oligomers by taking the potassium channel KcsA as an exemplary ion channel.
许多膜蛋白作为稳定的寡聚体发挥功能。了解引发和增强寡聚化的条件对于许多治疗方法都很重要。在这方面，蛋白质-蛋白质和蛋白质-脂质相互作用在寡聚复合物的组装和稳定性中起着至关重要的作用。近年来，关于细胞质末端在决定寡聚复合物亚基组装和稳定性中的重要性的机制信息迅速增加。此外，阴离子磷脂与蛋白质表面“热点”之间的特定蛋白-脂质相互作用在稳定寡聚体组装方面的作用也变得明显。本综述以钾通道 KcsA 为例，重点介绍了几种通过稳定寡聚体的膜蛋白的当代进展。
