Wilkins Marc R, Kummerfeld Sarah K
School of Biotechnology and Biomolecular Sciences, University of New South Wales, NSW 2052, Australia.
Trends Biochem Sci. 2008 May;33(5):195-200. doi: 10.1016/j.tibs.2008.03.001. Epub 2008 Apr 20.
Advances in techniques for the study of protein-protein interactions have dramatically improved our understanding of the interactome. However, we know little about the dynamics of this complex system. To better understand the dynamics of the interactome, it is important to consider what happens when single proteins are perturbed. Changes in protein abundance and post-translational modification can function as switches in the interactome, affecting protein-complex assembly and function. Changes in protein sequence or a dramatic increase in abundance might cause a promiscuous gain of interactions. These effects are not identical for all proteins and will differ depending on the number and type of interaction partners that a protein has.
蛋白质-蛋白质相互作用研究技术的进步极大地增进了我们对相互作用组的理解。然而,我们对这个复杂系统的动力学了解甚少。为了更好地理解相互作用组的动力学,考虑单个蛋白质受到扰动时会发生什么很重要。蛋白质丰度和翻译后修饰的变化可以作为相互作用组中的开关,影响蛋白质复合物的组装和功能。蛋白质序列的变化或丰度的急剧增加可能会导致相互作用的杂乱增加。这些影响并非对所有蛋白质都相同,并且会因蛋白质所具有的相互作用伙伴的数量和类型而异。