title: Signalling complexes at the cell-matrix interface.
abstract: 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 α5β1, αvβ3 and αIIbβ3 have been mapped in unprecedented detail. The structure of integrin αXβ2 has revealed how ligand binding to the α 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.
authors.affiliation: Department of Life Sciences, Imperial College London, Sir Ernst Chain Building, London SW7 2AZ, UK. Electronic address: e.hohenester@imperial.ac.uk.
authors.forename: Erhard
authors.initials: E
authors.lastname: Hohenester
mesh_terms: D000818:Animals; D001665:Binding Sites; D003600:Cytosol / Q000737:chemistry*; D000070818:Discoidin Domain Receptors; D005109:Extracellular Matrix / Q000737:chemistry*; D006801:Humans; D016023:Integrins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry*; D011975:Receptors, Mitogen / Q000737:chemistry*; D016608:Talin / Q000037:antagonists & inhibitors / Q000737:chemistry
chemical_list: D016023:Integrins; D011975:Receptors, Mitogen; D016608:Talin; D000070818:Discoidin Domain Receptors; D020794:Receptor Protein-Tyrosine Kinases