@article{f309a150596011dd8d9f000ea68e967b,
title = "Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation.",
abstract = "We have defined the molecular basis of cell adhesion to fibrillin-1, the major structural component of extracellular microfibrils that are associated with elastic fibres. Using human dermal fibroblasts, and recombinant domain swap fragments containing the Arg-Gly-Asp motif, we have demonstrated a requirement for upstream domains for integrin-alpha(5)beta(1)-mediated cell adhesion and migration. An adjacent heparin-binding site, which supports focal adhesion formation, was mapped to the fibrillin-1 TB5 motif. Site-directed mutagenesis revealed two arginine residues that are crucial for heparin binding, and confirmed their role in focal adhesion formation. These integrin and syndecan adhesion motifs juxtaposed on fibrillin-1 are evolutionarily conserved and reminiscent of similar functional elements on fibronectin, highlighting their crucial functional importance.",
author = "Bax, {Daniel V} and Yashithra Mahalingam and Stuart Cain and Kieran Mellody and Lyle Freeman and Kerri Younger and Shuttleworth, {C Adrian} and Humphries, {Martin J} and Couchman, {John R} and Kielty, {Cay M}",
note = "Keywords: Base Sequence; Binding Sites; Cell Adhesion; DNA Primers; Epidermal Growth Factor; Heparin; Integrin alpha5beta1; Microfilament Proteins; Mutagenesis, Site-Directed; Oligopeptides; Recombinant Proteins",
year = "2007",
doi = "10.1242/jcs.003954",
language = "English",
volume = "120",
pages = "1383--92",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",
number = "Pt 8",
}