title: The role of integrin binding sites in fibronectin matrix assembly in vivo.
abstract: The extracellular matrix (ECM) glycoprotein fibronectin (FN) requires the help of cells to assemble into a functional fibrillar matrix, which then orchestrates the assembly of other ECM proteins and promotes cell adhesion, migration and signalling. Fibrillogenesis is initiated and governed by cell surface integrins that bind to specific sites in the FN molecule. Recent studies identified novel integrin binding sites in FN that can also participate in FN fibril formation and in morphogenetic events during development.
authors.affiliation: Max Planck Institute of Biochemistry, Department of Molecular Medicine, 82152 Martinsried, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Leiss
authors.forename: Karsten
authors.initials: K
authors.lastname: Beckmann
authors.forename: Amparo
authors.initials: A
authors.lastname: Girós
authors.forename: Mercedes
authors.initials: M
authors.lastname: Costell
authors.forename: Reinhard
authors.initials: R
authors.lastname: Fässler
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism*; D005353:Fibronectins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D016023:Integrins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D005353:Fibronectins; D006497:Heparan Sulfate; D016023:Integrins