Anschutz A, Howlet A, Klein C
E. A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, MO 63104.
Proc Natl Acad Sci U S A. 1989 May;86(10):3665-8. doi: 10.1073/pnas.86.10.3665.
Increasing effort is directed toward elucidating the mechanisms by which guanine nucleotide-binding proteins regulate specific cellular processes. A common feature of this class of proteins is that GTP induces a transition from an inactive to an active conformation. The latter is limited by the hydrolysis of GTP and the coincident production of GDP. Here we provide evidence that guanine nucleotides may regulate biological processes by inducing the phosphorylation of specific proteins. In particular, we report a GDP-dependent phosphorylation of p36, a 36-kDa protein of Dictyostelium discoideum plasma membranes.
人们越来越致力于阐明鸟嘌呤核苷酸结合蛋白调节特定细胞过程的机制。这类蛋白质的一个共同特征是，鸟苷三磷酸（GTP）诱导其从无活性构象转变为活性构象。后者受到GTP水解和同时产生的鸟苷二磷酸（GDP）的限制。在这里，我们提供证据表明鸟嘌呤核苷酸可能通过诱导特定蛋白质的磷酸化来调节生物过程。特别是，我们报道了盘基网柄菌质膜上一种36 kDa蛋白质p36的GDP依赖性磷酸化。
