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The fibronectin-binding integrins alpha 5 beta 1 and alpha v beta 3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis

Danen, EHJ; Sonneveld, P; Brakebusch, Cord LU ; Fässler, Reinhard LU and Sonnenberg, A (2002) In Journal of Cell Biology 159(6). p.1071-1086
Abstract
We have studied the formation of different types of cell matrix adhesions in cells that bind to fibronectin via either alpha5beta1 or alphavbeta3. In both cases, cell adhesion to fibronectin leads to a rapid decrease in RhoA activity. However, alpha5beta1 but not alphavbeta3 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 alphavbeta3-mediated fibrillogenesis. Despite the fact that alpha5beta1-mediated adhesion to the central cell-binding domain of fibronectin supports activation of RhoA, other... (More)
We have studied the formation of different types of cell matrix adhesions in cells that bind to fibronectin via either alpha5beta1 or alphavbeta3. In both cases, cell adhesion to fibronectin leads to a rapid decrease in RhoA activity. However, alpha5beta1 but not alphavbeta3 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 alphavbeta3-mediated fibrillogenesis. Despite the fact that alpha5beta1-mediated adhesion to the central cell-binding domain of fibronectin supports activation of RhoA, other regions of fibronectin are required for the development of alpha5beta1-mediated but not alphavbeta3-mediatecl focal contacts. Using chimeras of beta1 and beta3 subunits, we find that the extracellular domain of beta1 controls RhoA activity. By expressing both beta1 and beta3 at high levels, we show that beta1-mediated control of the levels of beta3 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Rho-GTPase, integrin, cell matrix adhesion, fibronectin, matrix assembly
in
Journal of Cell Biology
volume
159
issue
6
pages
1071 - 1086
publisher
Rockefeller University Press
external identifiers
  • wos:000180150200016
  • pmid:12486108
  • scopus:0037164867
ISSN
0021-9525
DOI
10.1083/jcb.200205014
language
English
LU publication?
yes
id
bf9f5aa6-84e3-47a1-9c48-e60b557524d7 (old id 320661)
date added to LUP
2007-08-15 16:00:42
date last changed
2017-11-19 03:40:29
@article{bf9f5aa6-84e3-47a1-9c48-e60b557524d7,
  abstract     = {We have studied the formation of different types of cell matrix adhesions in cells that bind to fibronectin via either alpha5beta1 or alphavbeta3. In both cases, cell adhesion to fibronectin leads to a rapid decrease in RhoA activity. However, alpha5beta1 but not alphavbeta3 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 alphavbeta3-mediated fibrillogenesis. Despite the fact that alpha5beta1-mediated adhesion to the central cell-binding domain of fibronectin supports activation of RhoA, other regions of fibronectin are required for the development of alpha5beta1-mediated but not alphavbeta3-mediatecl focal contacts. Using chimeras of beta1 and beta3 subunits, we find that the extracellular domain of beta1 controls RhoA activity. By expressing both beta1 and beta3 at high levels, we show that beta1-mediated control of the levels of beta3 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.},
  author       = {Danen, EHJ and Sonneveld, P and Brakebusch, Cord and Fässler, Reinhard and Sonnenberg, A},
  issn         = {0021-9525},
  keyword      = {Rho-GTPase,integrin,cell matrix adhesion,fibronectin,matrix assembly},
  language     = {eng},
  number       = {6},
  pages        = {1071--1086},
  publisher    = {Rockefeller University Press},
  series       = {Journal of Cell Biology},
  title        = {The fibronectin-binding integrins alpha 5 beta 1 and alpha v beta 3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis},
  url          = {http://dx.doi.org/10.1083/jcb.200205014},
  volume       = {159},
  year         = {2002},
}