Hook S S, Means A R
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
Annu Rev Pharmacol Toxicol. 2001;41:471-505. doi: 10.1146/annurev.pharmtox.41.1.471.
Calmodulin (CaM) is an essential protein that serves as a ubiquitous intracellular receptor for Ca(2+). The Ca(2+)/CaM complex initiates a plethora of signaling cascades that culminate in alteration of cellular functions. Among the many Ca(2+)/CaM-binding proteins to be discovered, the multifunctional protein kinases CaMKI, II, and IV play pivotal roles. Our review focuses on this class of CaM kinases to illustrate the structural and biochemical basis for Ca(2+)/CaM interaction with and regulation of its target enzymes. Gene transcription has been chosen as the functional endpoint to illustrate the recent advances in Ca(2+)/CaM-mediated signal transduction mechanisms.
钙调蛋白(CaM)是一种重要蛋白质,作为细胞内普遍存在的钙离子受体。钙离子/钙调蛋白复合物启动大量信号级联反应,最终导致细胞功能改变。在众多已发现的钙离子/钙调蛋白结合蛋白中,多功能蛋白激酶CaMKI、II和IV发挥着关键作用。我们的综述聚焦于这类钙调蛋白激酶,以阐述钙离子/钙调蛋白与其靶酶相互作用及调控的结构和生化基础。基因转录已被选作功能终点,以说明钙离子/钙调蛋白介导的信号转导机制的最新进展。