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, fluorescence recovery after photobleaching (FRAP) analysis, and simulations t...

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Main Authors: Sieber, J, Willig, K, Kutzner, C, Gerding-Reimers, C, Harke, B, Donnert, G, Rammner, B, Eggeling, C, Hell, S, Grubmüller, H, Lang, T
Format: Journal article
Language:English
Published: 2007
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author Sieber, J
Willig, K
Kutzner, C
Gerding-Reimers, C
Harke, B
Donnert, G
Rammner, B
Eggeling, C
Hell, S
Grubmüller, H
Lang, T
author_facet Sieber, J
Willig, K
Kutzner, C
Gerding-Reimers, C
Harke, B
Donnert, G
Rammner, B
Eggeling, C
Hell, S
Grubmüller, H
Lang, T
author_sort Sieber, J
collection OXFORD
description 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.
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spelling oxford-uuid:8801f9a7-9483-4e22-9b0b-e12f812aca862022-03-26T22:14:17ZAnatomy and dynamics of a supramolecular membrane protein cluster.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8801f9a7-9483-4e22-9b0b-e12f812aca86EnglishSymplectic Elements at Oxford2007Sieber, JWillig, KKutzner, CGerding-Reimers, CHarke, BDonnert, GRammner, BEggeling, CHell, SGrubmüller, HLang, TMost 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.
spellingShingle Sieber, J
Willig, K
Kutzner, C
Gerding-Reimers, C
Harke, B
Donnert, G
Rammner, B
Eggeling, C
Hell, S
Grubmüller, H
Lang, T
Anatomy and dynamics of a supramolecular membrane protein cluster.
title Anatomy and dynamics of a supramolecular membrane protein cluster.
title_full Anatomy and dynamics of a supramolecular membrane protein cluster.
title_fullStr Anatomy and dynamics of a supramolecular membrane protein cluster.
title_full_unstemmed Anatomy and dynamics of a supramolecular membrane protein cluster.
title_short Anatomy and dynamics of a supramolecular membrane protein cluster.
title_sort anatomy and dynamics of a supramolecular membrane protein cluster
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