Journal
FEBS LETTERS
Volume 541, Issue 1-3, Pages 126-131Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00324-7
Keywords
fluorescence correlation spectroscopy; protein kinase C; green fluorescent protein; diffusion constant; signal transduction; plasma membrane
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We employed fluorescence correlation spectroscopy (FCS) to analyze the characteristics of biomolecules in living cells. Protein kinase C (PKC) changes its subcellular localization from cytosol to the plasma membrane by its ligand. Using FCS, we found PKCbetaI labeled with enhanced green fluorescent protein freely diffusing in cytosol. Upon 12-O-tetradecanoylphorbol-13-acetate activation, a large part of PKCbetaI is anchored in the plasma membrane but some PKCbetaI still moves freely near the plasma membrane. These results indicate that a diffusion-driven transport mechanism is appropriate for the molecular mechanism of the PKCbetaI localization change. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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