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Anatomy and Dynamics of a Supramolecular Membrane Protein Cluster

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, fluorescene recovery after photobleaching (FRAP) analysis, and simulations... Full description

1st Person: Sieber, Jochen J.
Additional Persons: Willig, Katrin I. verfasserin; Kutzner, Carsten verfasserin; Gerding-Reimers, Claas verfasserin; Harke, Benjamin verfasserin; Donnert, Gerald verfasserin; Rammner, Burkhard verfasserin; Eggeling, Christian verfasserin; Hell, Stefan W. verfasserin; Grubmüller, Helmut verfasserin; Lang, Thorsten verfasserin
Source: in Science Vol. 317, No. 5841 (2007), p. 1072-1076
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Type of Publication: Article
Language: English
Published: 2007
Keywords: research-article
Online: Volltext
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Summary: 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, fluorescene 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.
Item Description: Copyright: Copyright 2007 American Association for the Advancement of Science
Physical Description: Online-Ressource
ISSN: 1095-9203

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