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STIP1 a novel SNARE complex interactor, and its function during tumour cell migration and invasion

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Title: STIP1 a novel SNARE complex interactor, and its function during tumour cell migration and invasion
Author: Alibabai, Layla
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Coppolino, Marc
Abstract: Tumour cell invasion often involves the formation of invadopodia, filamentous-actin rich membrane protrusions, that mediate extracellular matrix (ECM) degradation. ECM degradation is accomplished via the targeted secretion of matrix metalloproteinases (MMPs), primarily Membrane-Type 1 Matrix Metalloproteinase (MT1-MMP). Previous studies have identified that the delivery of MT1-MMP to invadopodia in MDA-MB-231 cells involves a soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) complex, comprising Syntaxin 4 (Stx4), Synaptosomal-associated protein 23 (SNAP-23), and vesicle-associated membrane protein 2 (VAMP2). It remains unclear what mechanisms are responsible for regulating SNARE activity and complex assembly during invadopodia formation and tumour cell invasion. This thesis describes studies, using mass-spectrometry-based proteomics and biochemical approaches, of the novel association of Stress-induced phosphoprotein 1 (STIP1) with the Stx4-SNAP23-VAMP2 complex. CRISPR/Cas9-mediated knockdown of STIP1 perturbs tumour cell migration and invasion. Taken together, these results indicate that STIP1 associates with the SNAP23 SNARE complex and facilitates tumour cell migration and invasion.
Date: 2021-01
Rights: Attribution 4.0 International
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Attribution 4.0 International Except where otherwise noted, this item's license is described as Attribution 4.0 International