Abstract
Shaping, maintenance and repair of adult tissues require fine-tuning of cell-cell adhesion. α-catenin, a cytoplasmic adapter links the actin cytoskeleton to cell-cell junctions, plays a central role in regulation of the cell-cell adherence. This regulation requires binding of α-catenin to vinculin in a force dependent manner. By stretching single α-catenin construct using magnetic tweezers, we find that force in physiological range can expose the vinculin-binding sites buried in α-catenin, drastically promoting subsequent binding of the head domain of vinculin with a nanoMolar affinity. The bound vinculin head then irreversibly locks α-catenin in its unfolded conformations after force is released. The bound vinculin head can however be displaced at high forces > 30 pN, resulting in a biphasic force dependent binding of α-catenin to vinculin head. Further, we find that full-length vinculin also binds to mechanically unfolded α-catenin, implying release of the auto-inhibition conformation of full-length vinculin. Together, these results provide important insights into mechanosensing at cell-cell adherence.
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