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Src induces tumour metastasis mainly by reducing

2017-05-18 14:37:22 | 日記

Src induces tumour metastasis mainly by reducing adhesiveness and by regulating the actin cytoskeleton3. The semi-flexible polymers of filamentous actin (F-actin), which are assembled from monomeric actin subunits (G-actin), exert or resist forces to drive a large number of cellular processes, including changes in cell shape, cell mobility, cytokinesis and intracellular transport. In addition, actin filaments translate external forces into biochemical signalling events that guide cellular responses6. This has been largely studied in the context of tumour invasion and malignancy, where mechanical signals from the tumour microenvironment impact the metastatic cascade7. In turn, metastatic breast cells have lower stiffness than their healthy counterparts, which is largely determined by the cytoskeleton8,9. To perform these different functions, actin filaments organize into distinct architectures through the control of a multitude of actin-binding proteins (ABPs) strongly conserved between species10. Ena/VASP (enabled/vasodilator stimulated phosphoprotein) family proteins, including protein-enabled homologue (Mena), vasodilator-stimulated phosphoprotein (VASP) and Ena-VASP-like (EVL), associate with barbed ends of actin filaments. They appear to have different effects on F-actin, including favouring actin filament elongation through their anti-capping activity, inhibiting the formation of branched actin networks and promoting F-actin bundling11. Accordingly, Ena/VASP family members have distinct effects on cancer cell migration and metastasis. While EVL suppresses cell migration12, the Mena variant Mena (INV) drives invasion, intravasation and metastasis13. Other ABPs inhibit actin polymerization or stabilize actin filaments. In addition, some ABPs organize actin filaments into higher-order networks, by cross-linking actin filaments, or use F-actin as a scaffold, physical support or track, to promote contractility and generate tension
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