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Coauthor of research linking syntaxin-4–Munc18 interactions with tumor invasion. The study connected trafficking of a membrane protease with the ability of cancer cells to remodel their surroundings.^[ref]

The N-terminal 1–29 fragment and the 1–15 fragment inhibit invadopodium formation. Their values are around one fifth of the control, and gelatin degradation is strongly reduced too. Full-length t-SNARE, empty vector and the 15–29 fragment remain near control values. The images agree: the inhibitory fragments leave much more intact gelatin beneath the cells. The corresponding published syntaxin-4 study links this phenotype to impaired cargo trafficking.^[ref]

Syntaxin-4 is a membrane-associated SNARE protein involved in fusion at the plasma cell membrane. In regulated GLUT4 delivery, it participates with compatible partners in the fusion machinery that exposes transporters at the cell surface. Its presence identifies a possible component of that machinery; productive fusion also depends on assembly and regulation of the whole SNARE complex. ^[ref]