Talins and kindlins; partners in integrin-mediated adhesion
By D. Calderwood, Iain D. Campbell, D. Critchley. Nature reviews. Molecular cell biology, 2013
612 citations recorded by the source corpus.
Integrin receptors provide a dynamic, tightly-regulated link between the extracellular matrix (or cellular counter-receptors) and intracellular cytoskeletal and signalling networks, enabling cells to sense and respond to their chemical and physical environment. Talins and kindlins, two families of FERM–domain proteins, bind the cytoplasmic tail of integrins, recruit cytoskeletal and signalling proteins involved in mechanotransduction and synergize to activate integrin binding to extracellular ligands. New data reveal the domain structure of full-length talin, provide insights into talin-mediated integrin activation and show that RIAM recruits talin to the plasma membrane, whereas vinculin stabilizes talin in cell–matrix junctions. How kindlins act is less well-defined, but disease-causing mutations show that kindlins are also essential for integrin activation, adhesion, cell spreading and signalling.
Subfields: Cell Biology, Immunology and Allergy
View Paper: https://www.semanticscholar.org/paper/2985d8235082a6596105edee141f0e8563a7c9ba
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Citations in the corpus
- Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020, background): “The protein products of ITGB1, CD151, and FERMT1 physically interact at the cell surface to mediate integrin signaling (Calderwood et al., 2013; Hemler, 2005).”
- Integrin-mediated mechanotransduction (2016, background): “The talin rod domain contains two additional F-actin–binding sites (ABS2 and ABS3), 11 vinculin-binding sites (VBSs), and binding sites for regulatory proteins, including RIAM (Rap1–GTP-interacting adapter molecule), Kank (KN motif and ankyrin repeat domains) family proteins (whose functions are dis”