Qiao Feng, Bowie James U
U.S. Department of Energy (UCLA-DOE) Institute of Genomics and Proteomics, Molecular Biology Institute, Department of Chemistry and Biochemistry, UCLA, CA 90095, USA.
Sci STKE. 2005 May 31;2005(286):re7. doi: 10.1126/stke.2862005re7.
Protein-protein interactions are essential for the assembly, regulation, and localization of functional protein complexes in the cell. SAM domains are among the most abundant protein-protein interaction motifs in organisms from yeast to humans. Although SAM domains adopt similar folds, they are remarkably versatile in their binding properties. Some identical SAM domains can interact with each other to form homodimers or polymers. In other cases, SAM domains can bind to other related SAM domains, to non-SAM domain-containing proteins, and even to RNA. Such versatility earns them functional roles in myriad biological processes, from signal transduction to transcriptional and translational regulation. In this review, we describe the structural basis of SAM domain interactions and highlight their roles in the scaffolding of protein complexes in normal and pathological processes.
蛋白质-蛋白质相互作用对于细胞中功能性蛋白质复合物的组装、调节和定位至关重要。SAM结构域是从酵母到人类的生物体中最丰富的蛋白质-蛋白质相互作用基序之一。尽管SAM结构域具有相似的折叠方式，但它们在结合特性上具有显著的多样性。一些相同的SAM结构域可以相互作用形成同二聚体或聚合物。在其他情况下，SAM结构域可以与其他相关的SAM结构域、不含SAM结构域的蛋白质甚至RNA结合。这种多功能性使它们在从信号转导到转录和翻译调控的无数生物过程中发挥功能作用。在本综述中，我们描述了SAM结构域相互作用的结构基础，并强调了它们在正常和病理过程中蛋白质复合物支架作用中的作用。
