By using laser tweezers, the authors show that a single alpha-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 alpha-catenin, which unfolds and strongly binds F-actin.alpha-catenin is a crucial protein at cell junctions that provides connection between the actin cytoskeleton and the cell membrane. At adherens junctions (AJs), alpha-catenin forms heterodimers with beta-catenin that are believed to resist force on F-actin. Outside AJs, alpha-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 alpha-beta-catenin heterodimer does not resist force but instead slips along F-actin in the direction of force. Conversely, the action of 5 to 10 alpha-beta-catenin heterodimers together with force applied toward F-actin pointed end engaged a molecular switch in alpha-catenin, which unfolded and strongly bound F-actin as a cooperative catch bond. Similarly, an alpha-catenin homodimer formed an asymmetric catch bond with F-actin triggered by protein unfolding under force. Our data suggest that alpha-catenin clustering together with intracellular tension engage a fluid-to-solid phase transition at the membrane-cytoskeleton interface.

α-catenin switches between a slip and an asymmetric catch bond with F-actin to cooperatively regulate cell junction fluidity / Arbore, C; Sergides, M; Gardini, L; Bianchi, G; Kashchuk, A V; Pertici, I; Bianco, P; Pavone, F S; Capitanio, M. - In: NATURE COMMUNICATIONS. - ISSN 2041-1723. - ELETTRONICO. - 13:(2022), pp. 0-0. [10.1038/s41467-022-28779-7]

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

Arbore, C;Sergides, M;Gardini, L;Bianchi, G;Pertici, I;Bianco, P;Pavone, F S;Capitanio, M
2022

Abstract

By using laser tweezers, the authors show that a single alpha-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 alpha-catenin, which unfolds and strongly binds F-actin.alpha-catenin is a crucial protein at cell junctions that provides connection between the actin cytoskeleton and the cell membrane. At adherens junctions (AJs), alpha-catenin forms heterodimers with beta-catenin that are believed to resist force on F-actin. Outside AJs, alpha-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 alpha-beta-catenin heterodimer does not resist force but instead slips along F-actin in the direction of force. Conversely, the action of 5 to 10 alpha-beta-catenin heterodimers together with force applied toward F-actin pointed end engaged a molecular switch in alpha-catenin, which unfolded and strongly bound F-actin as a cooperative catch bond. Similarly, an alpha-catenin homodimer formed an asymmetric catch bond with F-actin triggered by protein unfolding under force. Our data suggest that alpha-catenin clustering together with intracellular tension engage a fluid-to-solid phase transition at the membrane-cytoskeleton interface.
13
0
0
Arbore, C; Sergides, M; Gardini, L; Bianchi, G; Kashchuk, A V; Pertici, I; Bianco, P; Pavone, F S; Capitanio, M
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/1289165
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 4
  • ???jsp.display-item.citation.isi??? 3
social impact