Article
Phosphorylation of a distinct structural form of phosphatidylinositol transfer protein alpha at Ser166 by protein kinase C disrupts receptor-mediated phospholipase C signaling by inhibiting delivery of phosphatidylinositol to membranes.
The Journal of biological chemistry - 5 Nov 2004
Morgan Clive P, Skippen Alison, Segui Bruno, Ball Andrew, Allen-Baume Victoria, Larijani Banafshe, Murray-Rust Judith, McDonald Neil, Sapkota Gopal, Morrice Nick, Cockcroft Shamshad
Abstract excerpt
Phosphatidylinositol transfer protein alpha (PITPalpha) participates in the supply of phosphatidylinositol (PI) required for many cellular events including phospholipase C (PLC) beta and gamma signaling by G-protein-coupled receptors and receptor-tyrosine kinases, respectively. Protein kinase C has been known to modulate PLC signaling by G-protein-coupled receptors and receptor-tyrosine kinases, although the...
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