RGD Reference Report - Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. - Rat Genome Database
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Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly.

Authors: Fasshauer, D  Eliason, W K  BrĂ¼nger, A T  Jahn, R 
Citation: Fasshauer D, etal., Biochemistry. 1998 Jul 21;37(29):10354-62.
RGD ID: 12793053
Pubmed: (View Article at PubMed) PMID:9671503
DOI: Full-text: DOI:10.1021/bi980542h

Assembly of the three neuronal membrane proteins synaptobrevin, syntaxin, and SNAP-25 is thought to be one of the key steps in mediating exocytosis of synaptic vesicles. In vivo and in vitro, these proteins form a tight complex. Assembly is associated with a large increase in alpha-helical content, suggesting that major structural and conformational changes are associated with the assembly reaction. Limited proteolysis by trypsin, chymotrypsin, and proteinase K of the ternary complex formed from recombinant proteins lacking their membrane anchors revealed a SDS-resistant minimal core. The components of this core complex were purified and characterized by N-terminal sequencing and mass spectrometry. They include a slightly shortened synaptobrevin fragment, C- and N-terminal fragments of SNAP-25, and a C-terminal fragment of syntaxin that is slightly larger than the previously characterized H3 domain. Recombinant proteins corresponding to these fragments are sufficient for assembly and disassembly. In addition, each of the two SNAP-25 fragments can individually form complexes with syntaxin and synaptobrevin, suggesting that they both contribute to the assembly of the SNARE complex. Upon complex assembly, a large increase in alpha-helical content is observed along with a significantly increased melting temperature (Tm). Like the full-length complex, the minimal complex tends to form an oligomeric species; global analysis of equilibrium ultracentrifugation data suggests a monomer-trimer equilibrium exists. These conserved biophysical properties may thus be of fundamental importance in the mechanism of membrane fusion.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Snap25  (synaptosome associated protein 25)
Stx1a  (syntaxin 1A)
Vamp2  (vesicle-associated membrane protein 2)


Additional Information