Berlin 2008 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 11: Transport Processes
BP 11.8: Vortrag
Dienstag, 26. Februar 2008, 17:00–17:15, C 243
Anomalous diffusion of transmembrane proteins due to oligomerization — •Ulrich Schmidt1, Markus Elsner2, Maria Smedh3, Tommy Nilsson3, and Matthias Weiss1 — 1Cellular Biophysics Group, Deutsches Krebsforschungszentrum, Bioquant Center, Im Neuenheimer Feld 267, 69120 Heidelberg — 2Cell Biology and Metabolism Branch, National Institutes of Health, USA — 3Dept. of Medical and Clinical Genetics, Inst. of BioMedicine, Sahlgrenska Academy, Gothenburg University, Sweden
Membrane proteins frequently form higher-order structures, e.g. oligomers, to facilitate their function and to assume proper subcellular localization. Oligomerization, however, alters the diffusion properties of participating individual proteins. Here, we have tested this aspect for membrane proteins undergoing a dynamic oligomerization process by means of computer simulations. We find that the diffusion of individual proteins becomes anomalous on short time scales with the anomality depending on the underlying binding kinetics and the number of binding sites per protein. In support of these theoretical results, we find via fluorescence correlation spectroscopy that a fluorescently tagged transmembrane Golgi enzyme is highly anomalous in vivo. This observation is consistent with the notion that Golgi-resident proteins oligomerize, presumably to maintain correct cisternal localization and to enhance enzymatic reactions.