Verdinez Jissele A, Sebag Julien A
Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, United States.
Fraternal Order of Eagles Diabetes Research Center, University of Iowa, Iowa City, IA, United States.
Front Neurosci. 2021 Aug 13;15:730417. doi: 10.3389/fnins.2021.730417. eCollection 2021.
Prokineticin receptors are GPCRs involved in several physiological processes including the regulation of energy homeostasis, nociception, and reproductive function. PKRs are inhibited by the endogenous accessory protein MRAP2 which prevents them from trafficking to the plasma membrane. Very little is known about the importance of post-translational modification of PKRs and their role in receptor trafficking and signaling. Here we identify 2 N-linked glycosylation sites within the N-terminal region of PKR2 and demonstrate that glycosylation of PKR2 at position 27 is important for its plasma membrane localization and signaling. Additionally, we show that glycosylation at position 7 results in a decrease in PKR2 signaling through Gα without impairing Gα signaling.
促动力蛋白受体是参与多种生理过程的G蛋白偶联受体,包括能量稳态调节、伤害感受和生殖功能。PKRs被内源性辅助蛋白MRAP2抑制,后者阻止它们转运到质膜。关于PKRs翻译后修饰的重要性及其在受体转运和信号传导中的作用,人们知之甚少。在这里,我们在PKR2的N端区域鉴定出2个N-糖基化位点,并证明PKR2第27位的糖基化对其质膜定位和信号传导很重要。此外,我们表明第7位的糖基化导致PKR2通过Gα的信号传导减少,而不损害Gα信号传导。