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Membrane ultrastructure modulates immune cell signaling
Author(s) -
Pralle Arnd,
Huang Heng,
Simsek Muhammed
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1019.6
Subject(s) - biophysics , membrane , fluorescence correlation spectroscopy , cell membrane , chemistry , cytoskeleton , force spectroscopy , lipid raft , membrane protein , membrane fluidity , microbiology and biotechnology , cell surface receptor , cell signaling , receptor , signal transduction , cell , biology , biochemistry , molecule , organic chemistry
Membrane lipids modulate the cell membrane ultra‐structure by promoting nanocluster formation, and by influencing the coupling of the membrane to the cytoskeleton. These in turn modulate the cell membrane signaling. Direct observation of the interplay of signaling and lipid nanodomains is challenging due to their small size and dynamic nature (bimFCS), Monte‐Carlo‐Simulations and optical trap based thermal noise imaging (TNI), to characterize the biophysics of the lipid nanodomains Combining total internal fluorescence microscopy with fluorescence correlation spectroscopy into bimFCS, we are able to measure the diffusion of membrane receptors on multiple length scales simultaneously. We characterize the receptor‐nanodomain interaction continuously on single cells while perturbing the cell through receptor dimerization. I will show how bimFCS measurements, combined with defined TNI to confine a single membrane protein to diffuse for seconds in a small area provides sufficient data for high resolutions maps of local diffusion, local attraction potentials and membrane stiffness. Using a GPI‐anchored protein to probe the cell membrane we detect domains of increased membrane stiffness, which also show increased viscosity and are the preferred location for the GPI‐anchored protein.