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The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.

http://www.ncbi.nlm.nih.gov/pubmed/19667197

The Sec1/Munc18 (SM) protein family regulates intracellular trafficking through interactions with individual SNARE proteins and assembled SNARE complexes. Revealing a common mechanism of this regulation has been challenging, largely because of the multiple modes of interaction observed between SM proteins and their cognate syntaxin-type SNAREs. These modes include binding of the SM to a closed conformation of syntaxin, binding to the N-terminal peptide of syntaxin, binding to assembled SNARE complexes, and/or binding to nonsyntaxin SNAREs. The SM protein Vps45p, which regulates endosomal trafficking in yeast, binds the conserved N-terminal peptide of the syntaxin Tlg2p. We used size exclusion chromatography and a quantitative fluorescent gel mobility shift assay to reveal an additional binding site that does not require the Tlg2p N-peptide. Characterization of Tlg2p mutants and truncations indicate that this binding site corresponds to a closed conformation of Tlg2p. Furthermore, the Tlg2p N-peptide competes with the closed conformation for binding, suggesting a fundamental regulatory mechanism for SM-syntaxin interactions in SNARE assembly and membrane fusion.

Pubmed ID: 19667197 RIS Download

Mesh terms: Binding, Competitive | Circular Dichroism | Electrophoretic Mobility Shift Assay | Immunoblotting | Kinetics | Models, Molecular | Mutation | Protein Binding | Protein Conformation | Protein Structure, Tertiary | Qa-SNARE Proteins | Recombinant Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Vesicular Transport Proteins

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