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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.

Original publication




Journal article



Publication Date





1072 - 1076


Amino Acid Motifs, Animals, Cell Membrane, Chemical Phenomena, Chemistry, Physical, Computer Simulation, Diffusion, Fluorescence Recovery After Photobleaching, Green Fluorescent Proteins, Immunoblotting, Microscopy, Confocal, Microscopy, Fluorescence, Models, Biological, Nanotechnology, PC12 Cells, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins, Syntaxin 1