期刊
NATURE REVIEWS MOLECULAR CELL BIOLOGY
卷 14, 期 8, 页码 503-517出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3624
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资金
- National Institutes of Health (NIH)
- Medical Research Council
- Wellcome Trust
- Cancer Research UK
- MRC [G0900052] Funding Source: UKRI
- Medical Research Council [G0900052] Funding Source: researchfish
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 mechano-transduction 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.
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