The Protein Kinase C-dependent Phosphorylation of Serine 166 Is Controlled by the Phospholipid Species Bound to the Phosphatidylinositol Transfer Protein α

The charge isomers of bovine brain PI-TPα (i.e. PI-TPαI containing a phosphatidylinositol (PI) molecule and PI-TPαII containing a phosphatidylcholine (PC) molecule) were phosphorylated in vitro by rat brain protein kinase C (PKC) at different rates. From the double-reciprocal plot, it was estimated...

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Veröffentlicht in:	The Journal of biological chemistry 2000-07, Vol.275 (28), p.21532-21538
Hauptverfasser:	van Tiel, Claudia M., Westerman, Jan, Paasman, Marten, Wirtz, Karel W.A., Snoek, Gerry T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Brain - metabolism Carrier Proteins - chemistry Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cattle Cytosol - enzymology Kinetics Membrane Proteins Mice Peptide Mapping Phosphatidylinositols - metabolism Phospholipid Transfer Proteins Phospholipids - metabolism Phosphorylation Protein Kinase C - isolation & purification Protein Kinase C - metabolism Rats Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Serine Substrate Specificity
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