A family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell-signalling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumour promoters.
Jaken, S. Protein kinase C and tumor promoters. Curr. Opin. Cell2 (1990) 192–197. [DOI] [PMID: 2194521]
Parekh, D.B., Ziegler, W. and Parker, P.J. Multiple pathways control protein kinase C phosphorylation. EMBO J.19 (2000) 496–503. [DOI] [PMID: 10675318]
Valledor, A.F., Xaus, J., Comalada, M., Soler, C. and Celada, A. Protein kinase Cepsilon is required for the induction of mitogen-activated protein kinase phosphatase-1 in lipopolysaccharide-stimulated macrophages. J. Immunol.164 (2000) 29–37. [DOI] [PMID: 10604989]
Lendenfeld, T. and Kubicek, C.P. Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei. Biochem. J.330 (1998) 689–694. [PMID: 9480876]
Brooks, S.P. and Storey, K.B. Protein kinase C from rainbow trout brain: identification and characterization of three isozymes. Biochem. Mol. Biol. Int.44 (1998) 259–267. [PMID: 9530509]
[EC 188.8.131.52 created 2005 (EC 184.108.40.206 part-incorporated 2005)]