Protein kinase C isozyme (PKC)

Protein kinase C isozymes are members of an AGC family of serine/threonine-specific kinases that regulate myriad cell functions by phosphorylating proteins at serine and threonine residues[1][4][7]. The human PKC family has at least 10 well-characterized isozymes, classified by structural features and activation requirements: conventional (calcium and diacylglycerol-dependent), novel (diacylglycerol-dependent only), and atypical (independent of both). These enzymes integrate signals from receptors to coordinate responses essential for cell fate decisions, and they are implicated as key drivers of disease processes such as carcinogenesis, immune dysregulation, cardiac remodeling, and neurological disorders. Drugs targeting PKC isoforms are in development for several indications, but therapeutic safety is complicated by isoform diversity and functional overlap[1][3][7][9][10].

Other names

PKC isozymesProtein kinase C familyConventional PKC (cPKC: α, βI, βII, γ)Novel PKC (nPKC: δ, ε, η, θ)Atypical PKC (aPKC: ζ, ι/λ)

Drugs may act as inhibitors (block kinase activity) - Activators (mimic diacylglycerol, promote PKC activation) - Allosteric regulators, competitive ATP-binding site antagonists