Protein Kinase C

Protein kinase C (PKC) refers to a family of serine/threonine protein kinases grouped by their activation mechanism. Classical or conventional PKCs (cPKC α-, βI-, βII- and γ-) are activated by phosphatidylserine in a calcium dependent manner and can bind diacylglycerol (DAG). The Ca²⁺ insensitive novel PKCs (nPKCs ε-, δ-, θ- and η- isotypes) are also activated by DAG and phosphatidylserine.

The atypical PKCs (aPKCs ι- and ζ-) 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.

External sources of pharmacological information for Protein Kinase C :

• IUPHAR Receptor Code

• BJP Guide

Literature for Protein Kinase C

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Cancer Research Product Guide

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Protein Kinase C Gene Data