Calcium Activated Phospholipid Dependent Kinase (CAPK), also known as Protein Kinase C (PKC), is an enzyme that plays a crucial role in cellular signaling and regulation of various physiological processes. CAPK is activated in response to increased intracellular calcium levels and the presence of specific phospholipids, such as diacylglycerol (DAG) or phosphatidylserine (PS).
CAPK belongs to the family of protein kinase C enzymes, which are a group of serine/threonine kinases involved in signal transduction pathways. It consists of multiple isoforms, each with distinct tissue distribution and cellular functions. CAPK isoforms are widely expressed in various tissues, including the brain, heart, and immune system.
When CAPK is activated, it undergoes conformational changes that allow it to bind to its target substrates and phosphorylate them. CAPK phosphorylates a wide range of proteins, including ion channels, transcription factors, enzymes, and other kinases, leading to changes in their activity, localization, and function.
The activation of CAPK is essential for many cellular processes, such as cell growth, proliferation, differentiation, apoptosis, and neurotransmitter release. It is also involved in the regulation of various physiological functions like smooth muscle contraction, immune response, insulin secretion, and synaptic plasticity.
Dysregulation of CAPK activity has been implicated in the pathogenesis of several diseases, including cancer, cardiovascular diseases, immune disorders, and neurological disorders. Therefore, understanding the mechanisms of CAPK activation and function is crucial for the development of targeted therapies for these conditions.
