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Coauthor of research on selective activation of cognate SNARE complexes by Sec1/Munc18 proteins. The study connected recognition among fusion components with control of membrane fusion.^[ref]

Munc18 denotes a Sec1-Munc18 family of proteins that regulate SNARE-dependent membrane fusion. Different isoforms interact with particular syntaxin-associated pathways; Munc18-1 is prominent in neuronal secretion, while Munc18c participates in other trafficking systems. Binding to a syntaxin and promoting productive fusion are separable activities. Reconstitution experiments test how these regulators favour assembly of the appropriate fusion machinery. ^[ref]

The S61/E62 and S75/Q76 pairs are especially important for the extra stimulation attributable to Munc18. Their replacement leaves basal lipid mixing broadly present but makes the red and blue traces much closer together. In contrast, replacement of R47/V48 or D57/Q58 retains strong stimulation. The S75/E78/T79 replacement retains a smaller enhancement, suggesting a partial contribution under these conditions.

Compare the Munc18-dependent increment with each construct's own baseline, rather than comparing red endpoints alone. These results identify functionally important regions; they do not prove that every altered side chain directly contacts Munc18. The original reconstitution experiments also support cognate-SNARE recognition.^[ref]