Institute of Applied Physics - Biophysics
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Mario Brameshuber


Phone: +43 - (0)1 - 58801 - 134896


Mario Brameshuber obtained his M.S. (Dipl.Ing.) in Biophysics at Johannes Kepler University of Linz where he developed a single molecule bleaching technique termed “TOCCSL” for the detection and quantification of molecular aggregates diffusing in the plasma membrane. He completed his Ph.D. study at Johannes Kepler University of Linz in the group of Gerhard Schütz where he demonstrated the existence of stable associates of GPI-anchored proteins in the membrane of living CHO cells. After graduation Mario Brameshuber continued postdoctoral work in Linz and then moved to Stanford with a Wilhelm Macke scholarship. There he joined the group of Mark M. Davis and did postdoctoral work on addressing molecular events during T-cell activation by using single molecule techniques. Mario Brameshuber is currently university assistant at the Vienna University of Technology, group of Gerhard Schütz, and lecturer at the Vienna Medical University.

His research focusses on general features of the structure of the cellular plasma membrane by applying single molecule fluorescence techniques. His study on the homo-association of mGFP-GPI revealed the existence of structures reminiscent of highly controversially debated lipid rafts. In collaboration with experts in the field of heat shock and receptor signaling he applies the single molecule bleaching technique TOCCSL on plasma membrane targeted proteins and lipids to study their association during cellular events and under various physiological conditions. Mario Brameshuber is also studying the plasma membrane distribution and structural concepts of the T cell receptor complex in quiescent and activated murine T cells by applying TOCCSL, single molecule tracking, super-resolution techniques like STORM and PALM, and FRET. He further develops these approaches for the demand on highly sophisticated live cell techniques operating at a molecular level in order to address specific questions within his research.


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