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Anatomy and Dynamics of a Supramolecular Membrane Protein Cluster
Jochen J. Sieber,1
Katrin I. Willig,2
Carsten Kutzner,3
Claas Gerding-Reimers,1
Benjamin Harke,2
Gerald Donnert,2
Burkhard Rammner,4
Christian Eggeling,2
Stefan W. Hell,2
Helmut Grubmüller,3
Thorsten Lang1
Abstract:
Most plasmalemmal proteins organize in submicrometer-sized clusterswhose architecture and dynamics are still enigmatic. With syntaxin1 as an example, we applied a combination of far-field opticalnanoscopy, biochemistry, fluorescence recovery after photobleaching(FRAP) analysis, and simulations to show that clustering canbe explained by self-organization based on simple physical principles.On average, the syntaxin clusters exhibit a diameter of 50 to60 nanometers and contain 75 densely crowded syntaxins thatdynamically exchange with freely diffusing molecules. Self-associationdepends on weak homophilic protein-protein interactions. Simulationssuggest that clustering immobilizes and conformationally constrainsthe molecules. Moreover, a balance between self-associationand crowding-induced steric repulsions is sufficient to explainboth the size and dynamics of syntaxin clusters and likely ofmany oligomerizing membrane proteins that form supramolecularstructures.
1 Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. 2 Department of Nanobiophotonics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. 3 Department of Theoretical and Computational Biophysics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. 4 Friedensallee 92, 22763 Hamburg, Germany.
To whom correspondence should be addressed. E-mail: tlang{at}gwdg.de
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