Protein Kinase-C-alpha
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Protein Kinase-C -> Protein Kinase-C-alpha
Protein Kinase-C-alpha Definition
Encoded by human PRKCA Gene (PKC Family), 672-aa 77-kDa Protein Kinase C-alpha is a calcium-activated (likely by the C2 domain), DAG-activated, phospholipid-dependent serine/threonine kinase containing 2 zinc-dependent phorbol-ester/DAG binding domains and a C2 domain that phosphorylates a range of cellular proteins. DAG markedly increases PKC sensitivity to calcium and phospholipids. PKC activation appears to be central in the induction of cellular responses to many ligand-receptor systems and to external stimuli. After GPCR stimulation, and triggered by PKC-dependent serine phosphorylation, RKIP dissociates from RAF1 to associate with and block GRK2 activity. By activating PKC, the receptor signal may be enhanced by removing a RAF1 inhibitor and blocking receptor internalization. A receptor for phorbol ester tumor promoters, PKC may interact with PRKCABP. (NCI)
Protein Kinase-C-alpha Synonyms
Protein Kinase C-Alpha, PKCA, PRKCA, Protein Kinase Calpha
Terms in Protein Kinase-C-alpha category
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