Agonist mobility on supported lipid bilayers affects Fas mediated death response.
Extrinsic apoptosis is initiated by recognition and clustering of the single-pass transmembrane proteins Fas ligand and Fas expressed at the surface of closely apposed lymphocytes and target cells, respectively. Since Fas-mediated death response was mainly studied with soluble antibodies, the mobility constraints for receptor activation by a membrane embedded agonist is not well understood. We explored this influence by stimulating apoptosis on functionalized supported lipid bilayers, where we quantified agonist mobility by z-scan fluorescence correlation spectroscopy. Using different lipid compositions, we show that the apoptotic response correlates with increased lateral mobility of the agonist in the lipid bilayer.
Instituto de Investigación Médica Mercedes y Martín Ferreyra (INIMEC), CONICET-Universidad Nacional de Córdoba, Friuli 2434, CC389, 5000 Córdoba, Argentina.
M Florencia
MF
Sánchez
Departamento de Química Biológica-IQUIBICEN, Facultad de Ciencias Exactas, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, Argentina.
Valeria
V
Levi
Max Planck Institute of Biochemistry, Cellular and Molecular Biophysics, Am Klopferspitz 18, 82152 Martinsried, Germany. Electronic address: weidemann@biochem.mpg.de.
Thomas
T
Weidemann
Instituto de Investigación Médica Mercedes y Martín Ferreyra (INIMEC), CONICET-Universidad Nacional de Córdoba, Friuli 2434, CC389, 5000 Córdoba, Argentina. Electronic address: dolorescarrer@immf.uncor.edu.
Dolores C
DC
Carrer
D017209:Apoptosis; D057809:HEK293 Cells; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D008560:Membrane Fluidity; D009068:Movement; D019014:fas Receptor / Q000819:agonists* / Q000378:metabolism*
C491901:FAS protein, human; D008051:Lipid Bilayers; D019014:fas Receptor
Apoptosis; Fas receptor; Fluorescence correlation spectroscopy; Functionalized surface; Supported lipid bilayer