6UPV

Alpha-E-catenin ABD-F-actin complex

Summary for 6UPV

• Entry DOI: 10.2210/pdb6upv/pdb
• EMDB information: 20843
• Descriptor: Catenin alpha-1, Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: alpha-catenin, catenin, actin, mechanobiology, mechanosensing, cytoskeleton, cell adhesion
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 7
• Total formula weight: 412048.40

Authors

Mei, L.,Alushin, G.M. (deposition date: 2019-10-18, release date: 2020-09-30, Last modification date: 2025-04-02)

Primary citation

Mei, L.,Espinosa de Los Reyes, S.,Reynolds, M.J.,Leicher, R.,Liu, S.,Alushin, G.M.
Molecular mechanism for direct actin force-sensing by alpha-catenin.
Elife, 9:-, 2020

PubMed Abstract: The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin's C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin's C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin.

PubMed: 32969337
DOI: 10.7554/eLife.62514

Experimental method

ELECTRON MICROSCOPY (3.2 Å)