Abstract
ABSTRACTTalins are cytoskeletal linker proteins that consist of an N-terminal head domain, a flexible neck region and a C-terminal rod domain made of 13 helical bundles. The head domain binds integrin β-subunit cytoplasmic tails, which triggers integrin conformational activation to increase affinity for extracellular matrix proteins. The rod domain links to actin filaments inside the cell to transmit mechanical loads and serves as a mechanosensitive signalling hub for the recruitment of many other proteins. The α-helical bundles function as force-dependent switches – proteins that interact with folded bundles are displaced when force induces unfolding, exposing previously cryptic binding sites for other ligands. This leads to the notion of a talin code. In this Cell Science at a Glance article and the accompanying poster, we propose that the multiple switches within the talin rod function to process and store time- and force-dependent mechanical and chemical information.
Highlights
Talin, the principal protein linking integrins and F-actin, has emerged as a key mechano-effector protein for integrin-mediated adhesion to the extracellular matrix (ECM) (Critchley, 2009; Klapholz and Brown, 2017)
The simplest version of the hypothesis that talin encodes information is that adhesions in mechanically stable environments store information in binary switches provided by individual talin helix bundle domains
At the core of each adhesive structure will be a scaffold comprised of talin molecules, with its composition and signalling outputs dictated by the binary switch patterns of each talin molecule in that macromolecular complex
Summary
The principal protein linking integrins and F-actin, has emerged as a key mechano-effector protein for integrin-mediated adhesion to the extracellular matrix (ECM) (Critchley, 2009; Klapholz and Brown, 2017). In this Cell Science at a Glance article and the accompanying poster, we propose that the multiple switches within the talin rod function to process and store time- and force-dependent mechanical and chemical information.
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