Pleased to present our latest work, where we show that the cell-cell adhesion protein afadin coopts mechanically-regulated elements of the cadherin-catenin complex to drive cytoskeletal engagement. biorxiv.org/content/10.1101/…
Oct 24, 2024 · 5:49 PM UTC
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In the context of an E-cadherin–β-catenin–αE-catenin–vinculin supra-complex, we find that afadin’s coiled-coil domain engages flexible αE-catenin segments implicated in catch-bonding and force-activated actin binding.
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Afadin bridges neighboring αE-catenin actin-binding domains, mediating clustering of cadherin-catenin complexes along individual F-actin strands. We find this is associated with nanoscale curvature in the filament.
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Collectively, we propose this enables afadin to promote persistent maximal cytoskeletal engagement at cell-cell junctions experiencing sustained high forces. Curved F-actin could also be enriched at high-force sites enriched with afadin, such as tri-cellular junctions.
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This was work was led by amazing postdoc Rui Gong, with important contributions from @mattabolic_rate and @XiaoyuSun_LIM .
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The paper also contains many other data, including a detailed biochemical dissection of the interplay between vinculin and afadin in modulating F-actin binding by the cadherin-catenin complex. Please check it out! biorxiv.org/content/10.1101/…
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