Odom A R, Stahlberg A, Wente S R, York J D
Departments of Pharmacology and Cancer Biology and of Biochemistry, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.
Science. 2000 Mar 17;287(5460):2026-9. doi: 10.1126/science.287.5460.2026.
Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP6). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae, designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP6, was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.
磷脂酶C和两种肌醇多磷酸（IP）激酶构成了一条信号通路，该通路通过生成肌醇六磷酸（IP6）来调节核信使核糖核酸的输出。酿酒酵母中此信号通路的肌醇1,4,5-三磷酸激酶，命名为Ipk2，被发现与转录复合物ArgR-Mcm1的调节因子Arg82相同。通过ArgR-Mcm1进行基因调控需要合成肌醇1,4,5,6-四磷酸，而非IP6。因此，磷脂酶C信号通路产生多种IP信使，可调节不同的核过程。这些结果揭示了IP信号激活可能控制基因表达的直接机制。
