scholarly journals 2P523 Molecular dynamics of membrane-binding protein in living cells analyzed by total internal reflection fluorescence correlation spectroscopy(52. Bio-imaging,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S426
Author(s):  
Yu Ohsugi ◽  
Mamoru Tamura ◽  
Masataka Kinjo
Keyword(s):  
Molecular Dynamics ◽  
Fluorescence Correlation Spectroscopy ◽  
Total Internal Reflection ◽  
Poster Session ◽  
Living Cells ◽  
Correlation Spectroscopy ◽  
Internal Reflection ◽  
Fluorescence Correlation ◽  
Meeting Program ◽  
Bio Imaging

ANALYSIS OF MEMBRANE-BINDING PROTEIN MOBILITY IN LIVING CELLS USING TOTAL INTERNAL REFLECTION FLUORESCENCE CORRELATION SPECTROSCOPY

2006 ◽  
Vol 01 (03) ◽  
pp. 293-299 ◽  
Author(s):  
Y. OHSUGI ◽  
MASATAKA KINJO
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Fluorescence Correlation Spectroscopy ◽  
Total Internal Reflection ◽  
Membrane Binding ◽  
Living Cells ◽  
Correlation Spectroscopy ◽  
Internal Reflection ◽  
Total Internal Reflection Fluorescence ◽  
Fluorescence Correlation

Total internal reflection fluorescence correlation spectroscopy (TIR-FCS) is an appropriate method for measuring diffusion constants and the number of fluorescent molecules very close to the coverglass surface. Recently, we have reported the application of TIR-FCS to cell biology, measuring membrane-binding farnesylated green fluorescent proteins (EGFP-F) in living cells. In this research, we measured the signal transduction molecule, protein kinase C (PKC), fused with EGFP in living HeLa cells by using TIR-FCS. We observed two different diffusional mobilities of PKCβII-EGFP, three-dimensional faster diffusion near the plasma membrane and slower lateral diffusion on the plasma membrane after adinosine tri phosphate (ATP) activation. These results indicate that it is possible to use TIR-FCS in the study of molecular dynamics and interactions of signal transduction proteins on the plasma membrane of the living cell.

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