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First published online 20 March 2007
doi: 10.1242/jcs.003954

Journal of Cell Science 120, 1383-1392 (2007)
Published by The Company of Biologists 2007
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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. Bax1,2, Yashithra Mahalingam3, Stuart Cain2, Kieran Mellody2, Lyle Freeman2, Kerri Younger2, C. Adrian Shuttleworth2, Martin J. Humphries2, John R. Couchman3 and Cay M. Kielty1,2,*

1 UK Centre for Tissue Engineering, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK
2 Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK
3 Faculty of Medicine, Imperial College London, Exhibition Road, London, SW7 2AZ, UK

* Author for correspondence (e-mail: cay.kielty{at}manchester.ac.uk)

Accepted 5 February 2007

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}5beta1-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.

Key words: Fibrillin-1, Cell adhesion, Integrins, Heparin, Syndecan-4, Fibronectin


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