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J Biol Chem, Vol. 274, Issue 22, 15440-15446, May 28, 1999
From the Department of Neurobiology, Max Planck Institute for
Biophysical Chemistry, D-37077 Göttingen, Germany
Assembly of soluble
N-ethylmaleimide-sensitive fusion attachment protein
receptor (SNARE) proteins between two opposing membranes is thought to
be the key event that initiates membrane fusion. Many new SNARE
proteins have recently been localized to distinct intracellular
compartments, supporting the view that sets of specific SNAREs are
specialized for distinct trafficking steps. We have now investigated
whether other SNAREs can form complexes with components of the synaptic
SNARE complex including synaptobrevin/VAMP 2, SNAP-25, and syntaxin 1. When the Q-SNAREs syntaxin 2, 3, and 4, and the R-SNARE endobrevin/VAMP
8 were used in various combinations, heat-resistant complexes were
formed. Limited proteolysis revealed that these complexes contained a
protease-resistant core similar to that of the synaptic complex. All
complexes were disassembled by the ATPase
N-ethylmaleimide-sensitive fusion protein and its cofactor
Mixed and Non-cognate SNARE Complexes
CHARACTERIZATION OF ASSEMBLY AND BIOPHYSICAL PROPERTIES
-SNAP. Circular dichroism spectroscopy showed that major conformational changes occur during assembly, which are associated with
induction of structure from unstructured monomers. Furthermore, no
preference for synaptobrevin was observed during the assembly of the
synaptic complex when endobrevin/VAMP 8 was present in equal
concentrations. We conclude that cognate and non-cognate SNARE
complexes are very similar with respect to biophysical properties, assembly, and disassembly, suggesting that specificity of membrane fusion in intracellular membrane traffic is not due to intrinsic specificity of SNARE pairing.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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