蛋白质磷酸化是细胞信号传递中的一个重要环节 ,其中MAPKs(Ser Thr蛋白激酶家族 )可使多种细胞膜及核蛋白磷酸化 ,是细胞对外界刺激 (如丝裂原 )反应的重要调控者。核糖体亚单位激酶RSK作为其重要的下游效应分子可被MAPKs家族的ERK蛋白激酶特异地磷酸化而激活。近年来的研究发现RSKs是MAPKs下游调节细胞生存和细胞周期的蛋白激酶 ,对其结构和活性的分析表明 ,它在细胞中具有重要的功能意义。本文将对RSKs的生物学活性进行综述。 Protein phosphorylation is an important part of cell signaling. Among them, MAPKs (Ser Thr protein kinase family) phosphorylate various cell membranes and nuclear proteins and are important regulators of cell responses to external stimuli such as mitogen. The ribosomal subunit kinase RSK, as an important downstream effector, can be activated by specific phosphorylation of the MAPKs family of ERK protein kinases. Recent studies have found that RSKs are protein kinases that regulate cell survival and cell cycle downstream of MAPKs. Analysis of their structure and activity shows that RSKs have important functional significance in cells. This article reviews the biological activities of RSKs.