Protein Kinase C, Models of
Protein kinase C is a class of protein kinases with 11 isozymes grouped into three subclasses (Newton 2001). The protein kinase C isozymes in the typical group are activated by calcium, diacylglycerol (DAG), and arachidonic acid (AA). The isozymes in the novel group are activated by DAG and AA, but not calcium. The atypical group of isozymes are insensitive to both DAG and calcium. Most models of PKC activity describe binding of calcium and one or two lipids to the PKC holoenzyme.
All of the protein kinase C isozymes have a similar catalytic domain, and most of the isozymes have two additional domains important for PKC activation: the C2 domain that binds two to three calcium ions and the C1 domain that binds lipids. One additional PKC isozyme is called PKMζ. This is the constitutively active, catalytic domain of typical PKC. This molecule is normally at low levels, and it is “activated” either by cleavage of typical PKC forms or by synthesis.
KeywordsAMPA Receptor Climbing Fiber Cerebellar Purkinje Cell mGlu5 Receptor Calcium Oscillation
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