Kasahara Takaoki, Okano Toshiyuki, Haga Tatsuya, Fukada Yoshitaka
Department of Biophysics and Biochemistry, Graduate School of Science, Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
J Neurosci. 2002 Sep 1;22(17):7321-5. doi: 10.1523/JNEUROSCI.22-17-07321.2002.
Light is a major environmental signal for entrainment of the circadian clock, but little is known about the intracellular phototransduction pathway triggered by light activation of the photoreceptive molecule(s) responsible for the phase shift of the clock in vertebrates. The chicken pineal gland and retina contain the autonomous circadian oscillators together with the photic entrainment pathway, and hence they represent useful experimental models for the clock system. Here we show the expression of G11alpha, an alpha subunit of heterotrimeric G-protein, in both tissues by cDNA cloning, Northern blot, and Western blot analyses. G11alpha immunoreactivity was colocalized with pinopsin in the chicken pineal cells and also with rhodopsin in the outer segments of retinal photoreceptor cells, suggesting functional coupling of G11alpha with opsins in the clock-containing photosensitive tissues. The physical interaction was examined by coimmunoprecipitation experiments, the results of which provided evidence for light- and GTP-dependent coupling between rhodopsin and G11alpha. To examine whether activation of endogenous G11 leads to a phase shift of the oscillator, Gq/11-coupled m1-type muscarinic acetylcholine receptor (mAChR) was ectopically expressed in the cultured pineal cells. Subsequent treatment of the cells with carbamylcholine (CCh), an agonist of mAChR, induced phase-dependent phase shifts of the melatonin rhythm in a manner very similar to the effect of light. In contrast, CCh treatment induced no measurable effect on the rhythm of nontransfected (control) cells or cells expressing G(i/o)-coupled m2-type mAChR, indicating selectivity of the G-protein activation. Together, our results demonstrate the existence of a G11-mediated opsin-signaling pathway contributing to the photic entrainment of the circadian clock.
光是昼夜节律时钟同步的主要环境信号,但对于由负责脊椎动物时钟相移的光感受分子的光激活所触发的细胞内光转导途径,人们了解甚少。鸡的松果体和视网膜含有自主的昼夜节律振荡器以及光同步途径,因此它们代表了用于时钟系统的有用实验模型。在这里,我们通过cDNA克隆、Northern印迹和Western印迹分析,展示了异源三聚体G蛋白的α亚基G11α在这两种组织中的表达。G11α免疫反应性在鸡松果体细胞中与视锥蛋白共定位,在视网膜光感受器细胞的外段中也与视紫红质共定位,这表明G11α与含时钟光合作用组织中的视蛋白存在功能偶联。通过共免疫沉淀实验检测了物理相互作用,其结果为视紫红质与G11α之间的光和GTP依赖性偶联提供了证据。为了研究内源性G11的激活是否会导致振荡器的相移,在培养的松果体细胞中异位表达了与Gq/11偶联的m1型毒蕈碱型乙酰胆碱受体(mAChR)。随后用mAChR激动剂氨甲酰胆碱(CCh)处理细胞,诱导褪黑素节律产生相位依赖性相移,其方式与光的作用非常相似。相比之下,CCh处理对未转染(对照)细胞或表达与G(i/o)偶联的m2型mAChR的细胞的节律没有可测量的影响,表明G蛋白激活具有选择性。总之,我们的结果证明了存在一条G11介导的视蛋白信号通路,该通路有助于昼夜节律时钟的光同步。