Details

Autor(en) / Beteiligte

• Huang, Derek L.
• Bax, Nicolas A.
• Buckley, Craig D.
• Weis, William I.
• Dunn, Alexander R.

Titel

Vinculin forms a directionally asymmetric catch bond with F-actin

Ist Teil von

• Science (American Association for the Advancement of Science), 2017-08, Vol.357 (6352), p.703-706

Ort / Verlag

United States: American Association for the Advancement of Science

Erscheinungsjahr

2017

Quelle

MEDLINE

Beschreibungen/Notizen

• Vinculin is an actin-binding protein thought to reinforce cell-cell and cell-matrix adhesions. However, how mechanical load affects the vinculin–F-actin bond is unclear. Using a single-molecule optical trap assay, we found that vinculin forms a force-dependent catch bond with F-actin through its tail domain, but with lifetimes that depend strongly on the direction of the applied force. Force toward the pointed (−) end of the actin filament resulted in a bond that was maximally stable at 8 piconewtons, with a mean lifetime (12 seconds) 10 times as long as the mean lifetime when force was applied toward the barbed (+) end. A computational model of lamellipodial actin dynamics suggests that the directionality of the vinculin–F-actin bond could establish long-range order in the actin cytoskeleton. The directional and force-stabilized binding of vinculin to F-actin may be a mechanism by which adhesion complexes maintain front-rear asymmetry in migrating cells.