Anatomy and dynamics of a supramolecular membrane protein cluster
2007 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Sieber, Jochen J.; Willig, Katrin I. ; Kutzner, Carsten; Gerding-Reimers, Claas; Harke, Benjamin; Donnert, Gerald; Rammner, Burkhard; Eggeling, Christian ; Hell, Stefan ; Grubmüller, Helmut ; Lang, Thorsten
- Abstract
- 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.
- Issue Date
- 2007
- Journal
- Science
- ISSN
- 0036-8075
- Language
- English