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JCS ePress online publication date 20 Mar 2007
doi: 10.1242/jcs.003954

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Research Article

Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation


Daniel V. Bax, Yashithra Mahalingam, Stuart Cain, Kieran Mellody, Lyle Freeman, Kerri Younger, C. Adrian Shuttleworth, Martin J. Humphries, John R. Couchman, and Cay M. Kielty*
* Author for correspondence (e-mail: cay.kielty{at}manchester.ac.uk)

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.


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