page_title: Phosphoinositide phospholipase C
section_title: Function
hierarchical_section_title: Phosphoinositide phospholipase C / Function
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 2fju code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 2fju code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 2fju registreert is.
context_page_description: Phosphoinositide phospholipase C is a family of eukaryotic intracellular enzymes that play an important role in signal transduction processes. These enzymes belong to a larger superfamily of Phospholipase C. Other families of phospholipase C enzymes have been identified in bacteria and trypanosomes. Phospholipases C are phosphodiesterases.
  Phospholipase Cs participate in phosphatidylinositol 4,5-bisphosphate metabolism and lipid signaling pathways in a calcium-dependent manner. At present, the family consists of six sub-families comprising a total of 13 separate isoforms that differ in their mode of activation, expression levels, catalytic regulation, cellular localization, membrane binding avidity and tissue distribution. All are capable of catalyzing the hydrolysis of PIP₂ into two important second messenger molecules, which go on to alter cell responses such as proliferation, differentiation, apoptosis, cytoskeleton remodeling, vesicular trafficking, ion channel conductance, endocrine function and neurotransmission.
context_section_description: Phospholipase C performs a catalytic mechanism, depleting PIP2 and generating inositol trisphosphate (IP₃) and diacylglycerol (DAG).
  Depletion of PIP2 inactivates numerous effector molecules in the plasma membrane, most notably PIP2 dependent channels and transporters responsible for setting the cell's membrane potential.
  The hydrolytic products also go on to modulate the activity of downstream proteins important for cellular signaling. IP3 is soluble, and diffuses through the cytoplasm and interacts with IP3 receptors on the endoplasmic reticulum, causing the release of calcium and raising the level of intracellular calcium.
  Further reading: Function of calcium in humans
  DAG remains within the inner leaflet of the plasma membrane due to its hydrophobic character, where it recruits protein kinase C (PKC), which becomes activated in conjunction with binding calcium ions. This results in a host of cellular responses through stimulation of calcium-sensitive proteins such as Calmodulin.
  Further reading: Function of protein kinase C
caption: activated rac1 bound to its effector phospholipase c beta 2
exif: {}