Protein Kinase C

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 Protein kinase C, commonly abbreviated to PKC, is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine 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 (DAG) or calcium ions (Ca2+).[1] Hence PKC enzymes play important roles in several signal transduction cascades.[2]


References

[1]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.

[2]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.

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