Talins and Kindlins: Partners in Integrin-Mediated Adhesion

Nat Rev Mol Cell Biol. 2013 Aug;14(8):503-17. doi: 10.1038/nrm3624. Epub 2013 Jul 17.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Adhesion / genetics
  • Cell Communication / genetics*
  • Cell Communication / physiology
  • Humans
  • Integrins / metabolism
  • Integrins / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Models, Biological
  • Multigene Family / physiology
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism
  • Neoplasm Proteins / physiology*
  • Protein Binding / physiology
  • Talin / genetics
  • Talin / metabolism
  • Talin / physiology*

Substances

  • FERMT1 protein, human
  • Integrins
  • Membrane Proteins
  • Neoplasm Proteins
  • Talin