Protein kinase C (PKC) is a family of enzymes that play crucial roles in various cellular processes by modifying and regulating the activity of target proteins. It is a type of serine/threonine kinase, meaning it phosphorylates serine and threonine residues on target proteins, leading to changes in their function or activity.
PKC is involved in numerous signaling pathways and is activated in response to different extracellular stimuli, including hormones, growth factors, and neurotransmitters. Upon activation, PKC phosphorylates target proteins, which can trigger a cascade of downstream events. These events can include changes in gene expression, alterations in cell metabolism, regulation of ion channel activity, and modulation of cell shape and motility.
The PKC family consists of several isoforms, including conventional PKCs (α, βI, βII, and γ), novel PKCs (δ, ε, η, and θ), and atypical PKCs (ζ and ι/λ). Each isoform has a unique tissue distribution, subcellular localization, and substrate specificity, allowing for specificity in their cellular functions.
Malfunction or dysregulation of PKC has been implicated in various diseases, including cancer, cardiovascular disorders, neurological disorders, diabetes, and immune disorders. Consequently, PKC has emerged as an attractive target for therapeutic intervention, and the development of PKC inhibitors has shown promise in preclinical and clinical studies.
In summary, protein kinase C is a family of enzymes that phosphorylates target proteins, leading to diverse cellular effects. It is a crucial player in signal transduction pathways and is involved in numerous physiological processes.
