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BP: Fachverband Biologische Physik

BP 7: Poster I

BP 7.5: Poster

Monday, March 23, 2009, 17:45–20:00, P3

Elucidating structure and domain formation of biomimetic lipid bilayers — •Kristian Boye¹, Gernot Guigas¹, Eszter Molnar², Martin Holzer³, Wolfgang Schamel², and Matthias Weiss¹ — ¹DKFZ - German Cancer Research Center, Heidelberg, Germany — ²Max Planck Institute for Immunobiology, Freiburg, Germany — ³Institute of Pharmaceutical Sciences, University of Freiburg, Germany

Membrane domains - also known as lipid rafts - are believed to be central to various functions of the cell, including signal transduction, lateral sorting, pathogen recognition and internalization processes. While the nature and stability of these domains in the living cell is still highly controversial, model membrane systems, such as giant unilamellar vesicles (GUVs), allow a direct observation of large, optically resolvable domains that result from the coexistence of two or more lipid phases.

We have used confocal fluorescence microscopy and fluorescence correlation spectroscopy to investigate the spatial and dynamic organization of lipids in artificially produced GUVs with lipid compositions mimicking that of the endoplasmic reticulum and that of the plasma membrane of T cells. In both cases, we observe domain formation and, in part, the formation of buds and tubules. We moreover have evidence that specific transmembrane protein complexes, like the one formed by the T cell receptor, partition into specific lipid subphases.