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.
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Literature for Protein Kinase C
A collection of over 750 products for cancer research, the guide includes research tools for the study of:
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A collection of over 400 products for kinase research, the listing includes inhibitors of:
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- Receptor Serine/Threonine Kinases