Abstract
As illustrated in Fig. 1, the binding of a hormone (H), neurotransmitter or growth factor to a receptor (R) in a membrane can activate a phosphoinositide-specific phospholipase C (PLC) that hydrolyzes phosphatidylinositol 4,5-bisphosphate (PEP2) into the two second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 diffuses through the cytoplasm and releases calcium ions from the endoplasmic reticulum (ER). The increase in the cytoplasmic concentration of Ca++ produces translocation of protein kinase C (PKC) to the plasma membrane and concomitant activation of this enzyme. Maximal activation of PKC requires DAG, which remains in the membrane, and an acidic lipid such as phosphatidylserine (PS). The requirement for PS suggests that basic residues on the protein (+ signs) interact with acidic lipids in the membrane. The membrane-bound, activated form of PKC then phosphorylates its membrane-bound substrates, which include the myristoylated alanine-rich C kinase substrate (MARCKS) and pp60src (Src).
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McLaughlin, S. et al. (1996). The Importance of Lipid-Protein Interactions in Signal Transduction Through the Calcium-Phospholipid Second Messenger System. In: Op den Kamp, J.A.F. (eds) Molecular Dynamics of Biomembranes. NATO ASI Series, vol 96. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61126-1_19
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