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          Institute: MPI für biophysikalische Chemie     Collection: Neurobiologie (Prof. Reinhard Jahn)     Display Documents



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ID: 16935.0, MPI für biophysikalische Chemie / Neurobiologie (Prof. Reinhard Jahn)
SNARE assembly and disassembly exhibit a pronounced hysteresis
Authors:Fasshauer, D.; Antonin, W.; Subramaniam, V.; Jahn, R.
Language:English
Date of Publication (YYYY-MM-DD):2002-02
Title of Journal:Nature Structural Biology
Volume:9
Issue / Number:2
Start Page:144
End Page:151
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:SNARE proteins are essential for intracellular membrane fusion of eukaryotes. Their assembly into stable four-helix bundles bridges membranes and may provide the energy for initiating membrane fusion. In vitro, assembly of soluble SNARE fragments is accompanied by major structural rearrangements that can be described as a folding reaction. The pathways and the thermodynamics of SNARE protein interactions, however, are not known. Here we report that assembly and dissociation of two distantly related SNARE complexes exhibit a marked hysteresis. The assembled and disassembled native states are separated by a kinetic barrier and cannot equilibrate on biologically relevant timescales. We suggest that the hysteresis is a hallmark of all SNARE complexes and that complex assembly and disassembly follow different pathways that may be independently controlled.
Comment of the Author/Creator:Date: 2002, FEB
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Reinhard Jahn / 190
MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
MPI für biophysikalische Chemie/AG Dirk Fasshauer
Identifiers:URL:http://www.nature.com/nsmb/journal/v9/n2/pdf/nsb75...
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