Aliases for PRKCG Gene
External Ids for PRKCG Gene
Previous Symbols for PRKCG Gene
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase is expressed solely in the brain and spinal cord and its localization is restricted to neurons. It has been demonstrated that several neuronal functions, including long term potentiation (LTP) and long term depression (LTD), specifically require this kinase. Knockout studies in mice also suggest that this kinase may be involved in neuropathic pain development. Defects in this protein have been associated with neurodegenerative disorder spinocerebellar ataxia-14 (SCA14). [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKCG Gene
PRKCG (Protein Kinase C, Gamma) is a Protein Coding gene. Diseases associated with PRKCG include spinocerebellar ataxia 14 and spinocerebellar ataxia type14. Among its related pathways are Signaling by FGFR and Signaling by FGFR. GO annotations related to this gene include protein kinase activity and calcium-dependent protein kinase C activity. An important paralog of this gene is PRKCB.
UniProtKB/Swiss-Prot for PRKCG Gene
Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component ARNTL/BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity).
Protein kinase C (PKC) refers to a family of serine/threonine protein kinases grouped by their activation mechanism. Classical or conventional PKCs (cPKC alpha-, betaI- , betaII- and gamma-) are activated by phosphatidylserine in a calcium dependent manner and can bind diacylglycerol (DAG). The Ca2+ insensitive novel PKCs (nPKCs epsilon-, delta-, theta- and eta- isotypes) are also activated by DAG and phosphatidylserine. The atypical PKCs (aPKCs iota- and zeta-) are insensitive to Ca2+, DAG and phorbol esters. All PKCs isoforms consist of a highly conserved catalytic domain connected to a regulatory domain via a hinge region. The physiological roles of PKCs are vast. This due to PKC phosphorylation and activation of multiple target proteins, which are involved in signal transduction pathways including, but not limited to, receptor desensitization, modulation of membrane structure events, regulation of transcription, regulation of cell growth, immune responses, and in learning and memory.