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A more recent version of this article appeared on October 1, 2003
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Submitted on January 27, 2003
Revised on May 7, 2003
Accepted on July 1, 2003
1 Department of Microbiology, University of Pennsylvania, Philadelphia, PA 19104
* Corresponding author. E-mail address: boettige{at}mail.med.upenn.edu.
The common model for integrin mediated signaling is based
on integrin clustering and the potential for that clustering to
recruit signaling molecules including FAK and src. The clustering model
for transmembrane signaling originated with the analysis of the EGF
receptor signaling and remains the predominant model. The roles for
substrate-bound ligand and ligand occupancy in
integrin-mediated signaling are less clear. A kinetic model was
established using HT1080 cells in which there was a linear relationship
between the strength of adhesion, the proportion of 
5
1
integrin that could be chemically cross-linked, and the number
of receptor-ligand bonds. This graded signal produced a similarly
graded response measured by the level of specific phosphorylation of
FAK Y397. FAK Y397 phosphorylation could also be induced by antibody
bound to the substrate. In contrast, clustering of 51 on
suspended cells with either antibody to 1 or by clustering of
soluble ligand bound to 51 induced the phosphorylation of FAK
Y861 but not Y397. There were no differences in signaling when
activating antibodies were compared with blocking antibodies, presence
or absence of ligand. Only tethering of 51 to the substrate was
required for induction of FAK Y397 phosphorylation.
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