Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation.
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Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation. / Bax, Daniel V; Mahalingam, Yashithra; Cain, Stuart; Mellody, Kieran; Freeman, Lyle; Younger, Kerri; Shuttleworth, C Adrian; Humphries, Martin J; Couchman, John R; Kielty, Cay M.
In: Journal of Cell Science, Vol. 120, No. Pt 8, 2007, p. 1383-92.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation.
AU - Bax, Daniel V
AU - Mahalingam, Yashithra
AU - Cain, Stuart
AU - Mellody, Kieran
AU - Freeman, Lyle
AU - Younger, Kerri
AU - Shuttleworth, C Adrian
AU - Humphries, Martin J
AU - Couchman, John R
AU - Kielty, Cay M
N1 - Keywords: Base Sequence; Binding Sites; Cell Adhesion; DNA Primers; Epidermal Growth Factor; Heparin; Integrin alpha5beta1; Microfilament Proteins; Mutagenesis, Site-Directed; Oligopeptides; Recombinant Proteins
PY - 2007
Y1 - 2007
N2 - 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.
AB - 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.
U2 - 10.1242/jcs.003954
DO - 10.1242/jcs.003954
M3 - Journal article
C2 - 17374638
VL - 120
SP - 1383
EP - 1392
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - Pt 8
ER -
ID: 5160728