α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity.

Autor: Arbore, C., Sergides, M., Gardini, L., Bianchi, G., Kashchuk, A. V., Pertici, I., Bianco, P., Pavone, F. S., Capitanio, M.
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Zdroj: Nature Communications; 3/3/2022, Vol. 13 Issue 1, p1-11, 11p
Abstrakt: α-catenin is a crucial protein at cell junctions that provides connection between the actin cytoskeleton and the cell membrane. At adherens junctions (AJs), α-catenin forms heterodimers with β-catenin that are believed to resist force on F-actin. Outside AJs, α-catenin forms homodimers that regulates F-actin organization and directly connect the cell membrane to the actin cytoskeleton, but their mechanosensitive properties are inherently unknown. By using ultra-fast laser tweezers we found that a single α-β-catenin heterodimer does not resist force but instead slips along F-actin in the direction of force. Conversely, the action of 5 to 10 α-β-catenin heterodimers together with force applied toward F-actin pointed end engaged a molecular switch in α-catenin, which unfolded and strongly bound F-actin as a cooperative catch bond. Similarly, an α-catenin homodimer formed an asymmetric catch bond with F-actin triggered by protein unfolding under force. Our data suggest that α-catenin clustering together with intracellular tension engage a fluid-to-solid phase transition at the membrane-cytoskeleton interface. By using laser tweezers, the authors show that a single α-catenin molecule does not resist force on F-actin. However, clustering of multiple molecules and force applied toward F-actin pointed end engage a molecular switch in α-catenin, which unfolds and strongly binds F-actin. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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