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Signalling complexes at the cell-matrix interface
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DOI：10.1016/j.sbi.2014.08.009.png)
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Abstract
En 中文
The extracellular matrix critically controls cell behaviour. Many cell-matrix interactions are mediated by transmembrane receptors of the integrin family. In the last two years, the structural changes resulting from ligand binding to integrins alpha 5 beta 1, alpha v beta 3 and alpha llb beta 3 have been mapped in unprecedented detail. The structure of integrin alpha X beta 2 has revealed how ligand binding to the alpha I domain is transmitted to the rest of the ectodomain. The structural characterisation of the cytosolic regulator talin has been continued, revealing how the integrin binding site is blocked in auto-inhibited talin. Finally, structures of the discoidin domain receptors DDR1 and DDR2 have begun to reveal how these atypical receptor tyrosine kinases become activated by the major matrix component collagen.
Keywords:
RECEPTOR TYROSINE KINASES
STRUCTURAL BASIS
INTEGRIN ACTIVATION
CRYSTAL-STRUCTURE
VINCULIN-BINDING
EXTRACELLULAR SEGMENT
COLLAGEN RECOGNITION
LIGAND-BINDING
TALIN ROD
DOMAIN
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