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Science 24 August 2007:
Vol. 317. no. 5841, pp. 1072 - 1076
DOI: 10.1126/science.1141727
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Reports

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{dagger}

Most plasmalemmal proteins organize in submicrometer-sized clusters whose architecture and dynamics are still enigmatic. With syntaxin 1 as an example, we applied a combination of far-field optical nanoscopy, biochemistry, fluorescence recovery after photobleaching (FRAP) analysis, and simulations to show that clustering can be explained by self-organization based on simple physical principles. On average, the syntaxin clusters exhibit a diameter of 50 to 60 nanometers and contain 75 densely crowded syntaxins that dynamically exchange with freely diffusing molecules. Self-association depends on weak homophilic protein-protein interactions. Simulations suggest that clustering immobilizes and conformationally constrains the molecules. Moreover, a balance between self-association and crowding-induced steric repulsions is sufficient to explain both the size and dynamics of syntaxin clusters and likely of many oligomerizing membrane proteins that form supramolecular structures.

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.

{dagger} To whom correspondence should be addressed. E-mail: tlang{at}gwdg.de

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