The membrane binding kinetics of full-length PKCα is determined by membrane lipid composition

• Published in: Biochimica et biophysica acta Vol. 1821; no. 11; pp. 1434 - 1442
• Main Authors: Pérez-Lara, Ángel, Egea-Jiménez, Antonio L., Ausili, Alessio, Corbalán-García, Senena, Gómez-Fernández, Juan C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2012
• Subjects: Animals; Cell Membrane - metabolism; Diglycerides - metabolism; dissociation; enzyme activity; fluorescence; Fluorescence Resonance Energy Transfer; Kinetics; ligands; lipid bilayers; Lipid Bilayers - metabolism; lipid composition; lipids; Membrane Lipids - metabolism; Models, Molecular; Phosphatidylcholines - metabolism; Phosphatidylinositol 4,5-Diphosphate - metabolism; Phosphatidylserines - metabolism; PIP2; PKCα; Protein Binding; protein kinase C; Protein Kinase C-alpha - isolation & purification; Protein Kinase C-alpha - metabolism; Protein Structure, Tertiary; Rapid kinetics; Spectrometry, Fluorescence; stopped-flow; Swine; stopped-flow; Rapid kinetics; POPC; POPS; PKC; PKCα; DOG; IP3; PIP2

Protein kinase Cα (PKCα) is activated by its translocation to the membrane. Activity assays show the importance of PIP2 in determining the specific activity of this enzyme. A FRET stopped flow fluorescence study was carried out to monitor the rapid kinetics of protein binding to model membranes cont...