Cassill J A, Whitney M, Joazeiro C A, Becker A, Zuker C S
Howard Hughes Medical Institute, University of California, San Diego, La Jolla 92093.
Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11067-70. doi: 10.1073/pnas.88.24.11067.
G protein-coupled receptors are regulated via phosphorylation by a variety of protein kinases. Recently, termination of the active state of two such receptors, the beta-adrenergic receptor and rhodopsin, has been shown to be mediated by agonist- or light-dependent phosphorylation of the receptor by members of a family of protein-serine/threonine kinases (here referred to as G protein-coupled receptor kinases). We now report the isolation of a family of genes encoding a set of Drosophila protein kinases that appear to code for G protein-coupled receptor kinases. These proteins share a high degree of sequence homology with the bovine beta-adrenergic receptor kinase. The presence of a conserved family of G protein-coupled receptor kinases in vertebrates and invertebrates points to the central role of these kinases in signal transduction cascades.
G蛋白偶联受体受多种蛋白激酶磷酸化调控。最近发现，β-肾上腺素能受体和视紫红质这两种此类受体的活性状态终止，是由蛋白丝氨酸/苏氨酸激酶家族成员（此处称为G蛋白偶联受体激酶）对受体进行激动剂或光依赖性磷酸化介导的。我们现在报告分离出一个果蝇蛋白激酶基因家族，这些基因似乎编码G蛋白偶联受体激酶。这些蛋白与牛β-肾上腺素能受体激酶具有高度的序列同源性。脊椎动物和无脊椎动物中保守的G蛋白偶联受体激酶家族的存在，表明这些激酶在信号转导级联反应中起核心作用。
