Journal
JOURNAL OF CELL BIOLOGY
Volume 216, Issue 1, Pages 93-100Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201605097
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Funding
- Intramural Research Program of the National Institutes of Health, National Institute of Dental and Craniofacial Research
- College of Arts and Sciences of Drexel University
- Department of Biology of Drexel University
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Primary human fibroblasts have the remarkable ability to use their nucleus like a piston, switching from low-to high-pressure protrusions in response to the surrounding three-dimensional (3D) matrix. Although migrating tumor cells can also change how they migrate in response to the 3D matrix, it is not clear if they can switch between high-and low-pressure protrusions like primary fibroblasts. We report that unlike primary fibroblasts, the nuclear piston is not active in fibrosarcoma cells. Protease inhibition rescued the nuclear piston mechanism in polarized HT1080 and SW684 cells and generated compartmentalized pressure. Achieving compartmentalized pressure required the nucleoskeleton-cytoskeleton linker protein nesprin 3, actomyosin contractility, and integrin-mediated adhesion, consistent with lobopodia-based fibroblast migration. In addition, this activation of the nuclear piston mechanism slowed the 3D movement of HT1080 cells. Together, these data indicate that inhibiting protease activity during polarized tumor cell 3D migration is sufficient to restore the nuclear piston migration mechanism with compartmentalized pressure characteristic of nonmalignant cells.
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