%A Limin Mao, John Q Wang %T Phosphorylation of group I metabotropic glutamate receptors in drug addiction and translational research %0 Journal Article %D 2016 %J Journal of Translational Neuroscience %J Journal of Translational Neuroscience %@ 2096-0689 %R 10.3868/j.issn.2096-0689.01.002 %P 17-23 %V 1 %N 1 %U {https://academic.hep.com.cn/jtn/EN/10.3868/j.issn.2096-0689.01.002 %8 2016-09-30 %X Protein phosphorylation is an important posttranslational modification of group I metabotropic glutamate receptors (mGluR1 and mGluR5 subtypes, mGluR1/5) which are widely distributed throughout the mammalian brain. Several common protein kinases are involved in this type of modification, including protein kinase A, protein kinase C, and extracellular signal-regulated kinase. Through constitutive and activity-dependent phosphorylation of mGluR1/5 at specific residues, protein kinases regulate trafficking, subcellular/subsynaptic distribution, and function of modified receptors. Increasing evidence demonstrates that mGluR1/5 phosphorylation in the mesolimbic reward circuitry is sensitive to chronic psychostimulant exposure and undergoes adaptive changes in its abundance and activity. These changes contribute to long-term excitatory synaptic plasticity related to the addictive property of drugs of abuse. The rapid progress in uncovering the neurochemical basis of addiction has fostered bench-to-bed translational research by targeting mGluR1/5 for developing effective pharmacotherapies for treating addiction in humans. This review summarizes recent data from the studies analyzing mGluR1/5 phosphorylation. Phosphorylation-dependent mechanisms in stimulant-induced mGluR1/5 and behavioral plasticity are also discussed in association with increasing interest in mGluR1/5 in translational medicine.