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Vol. 11, Issue 3, 1047-1060, March 2000
§
*Craniofacial Developmental Biology and Regeneration Branch,
National Institute of Craniofacial and Dental Research, National
Institutes of Health, Bethesda, Maryland; and This study establishes that the physical state of the extracellular
matrix can regulate integrin-mediated cytoskeletal
assembly and tyrosine phosphorylation to generate two distinct types of cell-matrix adhesions. In primary fibroblasts,
Department
of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot,
Israel
5
1 integrin associates mainly
with fibronectin fibrils and forms adhesions structurally distinct from
focal contacts, independent of actomyosin-mediated cell contractility.
These "fibrillar adhesions" are enriched in tensin, but contain low
levels of the typical focal contact components paxillin, vinculin, and
tyrosine-phosphorylated proteins. However, when the fibronectin is
covalently linked to the substrate, 51 integrin forms highly tyrosine-phosphorylated, "classical"
focal contacts containing high levels of paxillin and vinculin. These experiments indicate that the physical state of the matrix, not just
its molecular composition, is a critical factor in defining cytoskeletal organization and phosphorylation at adhesion sites. We
propose that molecular organization of adhesion sites is controlled by
at least two mechanisms: 1) specific integrins associate with their ligands in transmembrane complexes with appropriate cytoplasmic anchor proteins (e.g., fibronectin-51
integrin-tensin complexes), and 2) physical properties (e.g.,
rigidity) of the extracellular matrix regulate local tension at
adhesion sites and activate local tyrosine phosphorylation, recruiting
a variety of plaque molecules to these sites. These mechanisms generate
structurally and functionally distinct types of matrix adhesions in fibroblasts.
Present address: The Hematology Institute,
Tel-Aviv Medical Center, Tel-Aviv, Israel.
§
Corresponding author. E-mail address:
benny.geiger{at}weizmann.ac.il.
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