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SNARE assembly and disassembly exhibit a pronounced hysteresis

MPS-Authors
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Fasshauer,  D.
Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Antonin,  W.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Subramaniam,  V.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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599701.pdf
(Publisher version), 921KB

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Citation

Fasshauer, D., Antonin, W., Subramaniam, V., & Jahn, R. (2002). SNARE assembly and disassembly exhibit a pronounced hysteresis. Nature Structural Biology, 9(2), 144-151. Retrieved from http://www.nature.com/nsmb/journal/v9/n2/pdf/nsb750.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F454-A
Abstract
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.