Fina Marie E, Wang Junling, Vedula Pavan, Tang Hsin-Yao, Kashina Anna, Dong Dawei W
Department of Biomedical Sciences, School of Veterinary Medicines, University of Pennsylvania, Philadelphia, PA, United States.
Proteomics and Metabolomics Facility, The Wistar Institute, Philadelphia, PA, United States.
Front Cell Dev Biol. 2022 Jan 21;9:807345. doi: 10.3389/fcell.2021.807345. eCollection 2021.
Arginylation is a post-translational modification mediated by the arginyltransferase (Ate1). We recently showed that conditional deletion of Ate1 in the nervous system leads to increased light-evoked response sensitivities of ON-bipolar cells in the retina, indicating that arginylation regulates the G-protein signaling complexes of those neurons and/or photoreceptors. However, none of the key players in the signaling pathway were previously shown to be arginylated. Here we show that Gt1, G1, RGS6, and RGS7 are arginylated in the retina and RGS6 and RGS7 protein levels are elevated in Ate1 knockout, suggesting that arginylation plays a direct role in regulating their protein level and the G-protein-mediated responses in the retina.
精氨酰化是一种由精氨酰转移酶（Ate1）介导的翻译后修饰。我们最近发现，在神经系统中条件性敲除Ate1会导致视网膜上ON双极细胞的光诱发反应敏感性增加，这表明精氨酰化调节这些神经元和/或光感受器的G蛋白信号复合物。然而，之前并未发现该信号通路中的关键蛋白有被精氨酰化的情况。在此我们发现，Gt1、G1、RGS6和RGS7在视网膜中会被精氨酰化，且在Ate1基因敲除小鼠中RGS6和RGS7的蛋白水平升高，这表明精氨酰化在调节视网膜中它们的蛋白水平以及G蛋白介导的反应中发挥直接作用。
