View source for Protein Kinase C

Protein kinase C, commonly abbreviated to PKC, is a family of [[Protein kinase|protein kinase]] [[Enzyme|enzymes]] that are involved in controlling the function of other [[Proteins|proteins]] through the [[Phosphorylation|phosphorylation]] of [[Hydroxyl groups|hydroxyl groups]] of [[Serine|serine]] and [[Threonine|threonine]] [[Amino acid|amino acid]] residues on these proteins, or a member of this family. PKC enzymes in turn are activated by signals, such as increases in the concentration of [[Diacylglycerol|diacylglycerol]] (DAG) or [[Calcium ions|calcium ions]] (Ca<sup>2+</sup>)<ref>Wilson CH, Ali ES, Scrimgeour N, Martin AM, Hua J, Tallis GA, Rychkov GY, Barritt GJ (2015). "Steatosis inhibits liver cell store-operated Ca²⁺ entry and reduces ER Ca²⁺ through a protein kinase C-dependent mechanism". The Biochemical Journal. 466 (2): 379–90.</ref>. Hence PKC enzymes play important roles in several [[Signal transduction|signal transduction cascades]]<ref>Ali ES, Hua J, Wilson CH, Tallis GA, Zhou FH, Rychkov GY, Barritt GJ (2016). "The glucagon-like peptide-1 analogue exendin-4 reverses impaired intracellular Ca2+ signalling in steatotic hepatocytes". BBA − Molecular Cell Research. 1863: 2135–46.</ref>.<br> 

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