PRKCG Protein, Human (Active, sf9, GST)

PKC gamma is a calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues. It regulates neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1 by increasing plasma membrane-associated GRIA4 expression, modulates sensitivity to opiates, pain, and alcohol, mediates synaptic function and cell survival after ischemia, and inhibits gap junction activity following oxidative stress. In primary cerebellar neurons, PKC gamma acts downstream of metabotropic glutamate receptor GRM5/MGLUR5, phosphorylating GRIN1/NMDAR1, which is critical for synaptic plasticity, synaptogenesis, excitotoxicity, and learning. While potentially involved in hippocampal long-term potentiation (LTP), it may not be essential for synaptic plasticity. PKC gamma contributes to desensitization of μ-opioid receptor-mediated G-protein activation in the spinal cord and is crucial for morphine-induced reinforcing effects in the limbic forebrain. It modulates μ-opioid receptor functionality via a signaling pathway leading to receptor phosphorylation and degradation, and may influence chronic morphine-induced nociceptive changes. The kinase also plays roles in neuropathic pain and maintains allodynia from peripheral inflammation. It mediates ethanol's behavioral effects and impacts on GABA(A) receptors, affecting initial sensitivity and tolerance. During cerebral ischemia, PKC gamma regulates neurotransmission and cell survival in synaptic membranes, participating in insulin-induced necrosis inhibition to minimize ischemic injury. It is required for eliminating multiple climbing fibers during cerebellar Purkinje cell innervation. In lens epithelial cells, hydrogen peroxide activates PKC gamma, which phosphorylates connexin-43 (GJA1/CX43), disassembling gap junction plaques and inhibiting activity—potentially protecting against oxidative stress (by similar). PKC gamma phosphorylates p53/TP53, promoting DNA damage-induced apoptosis, and resets the cerebral cortex circadian clock during restricted feeding by stabilizing BMAL1 via interference with ubiquitination (by similar). Additionally, it phosphorylates and activates LRRK1, which in turn phosphorylates RAB proteins involved in intracellular trafficking.