Yaffe Michael B
Center for Cancer Research, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA.
Biochem J. 2004 Apr 15;379(Pt 2):e1-2. doi: 10.1042/BJ20040284.
Serine/threonine phosphorylation plays a central role in cellular regulation, either by altering a protein's activity directly or by inducing specific protein-protein interactions, which, in turn, affect localization, binding specificity or activity. One group of molecules that bind to phosphoserine/phosphothreonine-containing sequences are the 14-3-3 proteins, which regulate a wide range of cellular targets. A new analysis of the 14-3-3 phosphoproteome using affinity chromatography has revealed many previously unknown 14-3-3 ligands whose binding to 14-3-3 proteins is phosphorylation-dependent. This study paves the way for future work on these important 14-3-3-interacting proteins.
丝氨酸/苏氨酸磷酸化在细胞调节中起着核心作用，它可以直接改变蛋白质的活性，也可以诱导特定的蛋白质-蛋白质相互作用，进而影响蛋白质的定位、结合特异性或活性。一类与含磷酸丝氨酸/磷酸苏氨酸序列结合的分子是14-3-3蛋白，它们调节广泛的细胞靶点。一项使用亲和色谱法对14-3-3磷酸化蛋白质组进行的新分析揭示了许多以前未知的14-3-3配体，它们与14-3-3蛋白的结合是磷酸化依赖性的。这项研究为今后对这些重要的与14-3-3相互作用的蛋白质的研究铺平了道路。
