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In situ observation of mobility and anchoring of PKCβI in plasma membrane
Author(s) -
Saito Kenta,
Ito Eiko,
Takakuwa Yuichi,
Tamura Mamoru,
Kinjo Masataka
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00324-7
Subject(s) - protein kinase c , cytosol , membrane , biophysics , chemistry , subcellular localization , microbiology and biotechnology , fluorescence , fluorescence correlation spectroscopy , biochemistry , enzyme , biology , cytoplasm , molecule , physics , organic chemistry , quantum mechanics
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 PKCβI labeled with enhanced green fluorescent protein freely diffusing in cytosol. Upon 12‐ O ‐tetradecanoylphorbol‐13‐acetate activation, a large part of PKCβI is anchored in the plasma membrane but some PKCβI still moves freely near the plasma membrane. These results indicate that a diffusion‐driven transport mechanism is appropriate for the molecular mechanism of the PKCβI localization change.