Megan I. Brasher Created 2026-10-20 Updated 2026-11-05
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]
MT1-MMP Created 2026-10-20 Updated 2026-11-05
MT1-MMP, also called MMP14, is a membrane-associated metalloprotease involved in remodelling the extracellular matrix. Surface delivery concentrates proteolytic activity at particular cellular locations, linking vesicle trafficking to matrix interactions. Altered total protein abundance and altered delivery to the surface are different routes to changing extracellular activity. This distinction matters when relating a trafficking perturbation to cell invasion. [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]
Syntaxin4-Munc18c Interaction Promotes Breast Tumor Invasion and Metastasis by Regulating MT1-MMP Trafficking by Megan I. Brasher and others. Results: N-terminal fragments reduce invadopodium formation and matrix degradation