Protein kinase C

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Protein kinase C also known as PKC () is a family of 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. PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol or Ca<sup>2+</sup>. Hence PKC enzymes play important roles in several signal transduction cascades.

The PKC family consists of about ten isozymes. Conventional (c)PKCs contain the isoforms α, β<sub>I</sub>, β<sub>II</sub>, and γ. These require Ca<sup>2+</sup>, diacylglycerol (DAG), and a phospholipid such as phosphatidylserine for activation. Novel (n)PKCs include the δ, ε, η, and θ isoforms, and require DAG, but do not require Ca<sup>2+</sup> for activation. Thus, conventional and novel PKCs are activated through the same signal transduction pathway as phospholipase C. On the other hand, atypical (a)PKCs (including protein kinase Mζ and ι / λ isoforms) require neither Ca<sup>2+</sup> nor diacylglycerol for activation. The term "protein kinase C" usually refers to the entire family of...... ...
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