Premium
A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains
Author(s) -
Margittai Martin,
Otto Henning,
Jahn Reinhard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00028-9
Subject(s) - synaptobrevin , syntaxin 3 , syntaxin , snare complex , transmembrane protein , exocytosis , transmembrane domain , chemistry , stx1a , lipid bilayer fusion , membrane protein , microbiology and biotechnology , biophysics , biochemistry , biology , amino acid , membrane , synaptic vesicle , vesicle , receptor
The proteins synaptobrevin (VAMP), SNAP‐25 and syntaxin 1 are essential for neuronal exocytosis. They assemble into a stable ternary complex which is thought to initiate membrane fusion. In vitro, the transmembrane domains of syntaxin and synaptobrevin are not required for association. Here we report a novel interaction between synaptobrevin and syntaxin that requires the presence of the transmembrane domains. When co‐reconstituted into liposomes, the proteins form a stable binary complex that cannot be disassembled by NSF and that is resistant to denaturation by SDS. Cleavage of synaptobrevin with tetanus toxin does not affect the interaction. Furthermore, the complex is formed when a truncated version of syntaxin is used that contains only 12 additional amino acid residues outside the membrane anchor. We conclude that the interaction is mediated by the transmembrane domains.