| Literature DB >> 12706832 |
Kenta Saito1, Eiko Ito, Yuichi Takakuwa, Mamoru Tamura, Masataka Kinjo.
Abstract
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.Entities:
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Year: 2003 PMID: 12706832 DOI: 10.1016/s0014-5793(03)00324-7
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124