Protein kinase C

Protein kinase C (PKC) is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or the members of PKC family. PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+).

Function

PKC is involved in several signal transduction cascades. The PKC enzymes are known to be involved in many different cellular functions, including cell growth and differentiation, gene expression, hormone secretion and membrane function.

Structure

PKC family members are known to be structurally similar to each other. They are all single polypeptide chains that are divided into a regulatory domain and a catalytic domain.

Isoforms

There are at least 12 known isoforms of PKC that are divided into three groups based on their second messenger requirements: conventional (or classical), novel, and atypical.

Role in disease

PKC is implicated in several disease states. It is thought to play a role in the development of cancer, and is also implicated in conditions such as Alzheimer's disease and bipolar disorder.

See also

• Protein kinase
• Signal transduction
• Phosphorylation
• Diacylglycerol
• Calcium ions
• Alzheimer's disease
• Bipolar disorder

References

Protein kinase C Resources
Latest articles Most recent articles Ongoing trials	Wikipedia