Department of Protein Structure, Institute of Physiology Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Physiol Res. 2014;63(Suppl 1):S155-64. doi: 10.33549/physiolres.932659.
Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin.
许多蛋白质功能调节的方面都需要特定的蛋白质-蛋白质相互作用来执行精确的生化和细胞功能。14-3-3 蛋白家族的高度保守成员介导这种相互作用,并通过与数百种其他蛋白质结合,提供多种调节功能,从而在许多细胞过程中发挥关键作用。14-3-3 蛋白结合可以通过多种方式影响靶蛋白的功能,包括调节其酶活性、亚细胞定位、结构和稳定性,或分子相互作用。在这篇综述中,我们重点介绍了三种重要的 14-3-3 结合伙伴(酵母中性海藻糖酶 Nth1、G 蛋白信号调节因子 3(RGS3)和 phosducin)的 14-3-3 蛋白依赖性调节机制。