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Published online 16 December 2002. doi:10.1083/jcb.200205014
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© The Rockefeller University Press, 0021-9525/2002/12/1071 $5.00
The Journal of Cell Biology, Volume 159, Number 6, 1071-1086

Article

 The fibronectin-binding integrins {alpha}5ß1 and {alpha}vß3 differentially modulate RhoA–GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis

Erik H.J. Danen1, Petra Sonneveld1, Cord Brakebusch2, Reinhard Fässler2 and Arnoud Sonnenberg1

1 Division of Cell Biology, Netherlands Cancer Institute, 1066 CX Amsterdam, Netherlands
2 Department of Experimental Pathology, Lund University Hospital, 22185 Lund, Sweden

Address correspondence to Arnoud Sonnenberg, Div. of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands

We have studied the formation of different types of cell matrix adhesions in cells that bind to fibronectin via either {alpha}5ß1 or {alpha}vß3. In both cases, cell adhesion to fibronectin leads to a rapid decrease in RhoA activity. However, {alpha}5ß1 but not {alpha}vß3 supports high levels of RhoA activity at later stages of cell spreading, which are associated with a translocation of focal contacts to peripheral cell protrusions, recruitment of tensin into fibrillar adhesions, and fibronectin fibrillogenesis. Expression of an activated mutant of RhoA stimulates {alpha}vß3-mediated fibrillogenesis. Despite the fact that {alpha}5ß1-mediated adhesion to the central cell-binding domain of fibronectin supports activation of RhoA, other regions of fibronectin are required for the development of {alpha}5ß1-mediated but not {alpha}vß3-mediated focal contacts. Using chimeras of ß1 and ß3 subunits, we find that the extracellular domain of ß1 controls RhoA activity. By expressing both ß1 and ß3 at high levels, we show that ß1-mediated control of the levels of ß3 is important for the distribution of focal contacts. Our findings demonstrate that the pattern of fibronectin receptors expressed on a cell dictates the ability of fibronectin to stimulate RhoA-mediated organization of cell matrix adhesions.

Key Words: integrin; Rho–GTPase; fibronectin; cell matrix adhesion; matrix assembly


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