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Signaling by Inositol Phospholipids

Signaling by Inositol Phospholipids. SIGMA-ALDRICH. Signaling by Inositol Phospholipids

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Signaling by Inositol Phospholipids

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  1. Signaling by Inositol Phospholipids SIGMA-ALDRICH

  2. Signaling by Inositol Phospholipids When bound by nerve growth factor (NGF), the high affinity NGF receptor, TrkA, autophosphorylates tyrosine residues in its cytoplasmic domain. The activated receptor binds to and activates phospholipase C (PLC), which cleaves membrane-bound phosphatidylinositol-bisphosphate (PIP2) to generate D-myo-inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 diffuses from the plasma membrane to its receptor on the surface of the endoplasmic reticulum (ER) that is coupled to a Ca2+-release channel in the ER membrane. There it stimulates the release of Ca2+ from ER stores resulting in an increase in the cytosolic concentration of Ca2+. Cytosolic Ca2+ is then available for binding to calmodulin or to various Ca2+-binding cytoskeletal proteins involved in microtubule and intermediate filament formation. Many of the enzymatic effects of the released Ca2+ are mediated through protein phosphorylations catalyzed by a family of Ca2+/calmodulin dependent protein kinases (CaMK-II/IV). References Carpenter, G., and Ji, Q.S., Phospholipase C as a signal-transducing element. Exp. Cell Res., 253, 15-24 (1999). Patel, S., et al., Molecular properties of inositol 1,4,5-trisphosphate receptors. Cell Calcium, 25, 247-264 (1999). Takei, K., et al., Regulation of nerve growth mediated by inositol 1,4,5-trisphosphate receptors in growth cones. Science, 282, 1705-1708 (1998).

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