Protein kinase c
From Wikipedia, the free encyclopedia
Protein Kinase C (also known as PKC, Ca+2-dependent protein kinase or C-kinase) is a serine/threonine protein kinase.
[edit] PKC and the phospholipase-C pathway
Protein Kinase C is activated by the phospholipase-C pathway. Calcium ions released into the cytosol by IP3 cause PKC to be translocated to the plasma membrane. Here it is activated by diacylglycerol (DAG), calcium ions and certain membrane phospholipids. Four out of the 10 known PKC isozymes are activated by DAG.
It is thought that the activation of PKC causes the phosphorylation of ion channels, especially in the brain. In many cells PKC increases gene transcription of certain genes. In one cascade, PKC leads to the phosphorylation of a DNA-bound regulatory protein.
