Hamaneh Mehdi Bagheri, Buck Matthias
Structure. 2008 Oct 8;16(10):1439-41. doi: 10.1016/j.str.2008.09.003.
Ras superfamily guanine nucleotide-binding proteins, such as G-proteins and small GTPases, are a paradigm for two-state molecular switches in cell signaling. Recent experimental and theoretical studies question this simple model. Now Chen et al. (2008) provide evidence that the rgRGS domain of PDZRhoGEF has evolved to “trip” the nucleotide-dependent switch of the subunit of the heterotrimeric G-protein, Gα13, so that it can also bind to its GDP state.
Ras超家族鸟嘌呤核苷酸结合蛋白，如G蛋白和小GTP酶，是细胞信号传导中双态分子开关的范例。最近的实验和理论研究对这个简单模型提出了质疑。现在，陈等人（2008年）提供证据表明，PDZRhoGEF的rgRGS结构域已经进化到能“触发”异三聚体G蛋白Gα13亚基的核苷酸依赖性开关，使其也能结合到其GDP状态。
