Functional β1-integrins release the suppression of fibronectin matrix assembly by vitronectin

Qinghong Zhang, Takao Sakai, Julie Nowlen, Izumi Hayashi, Reinhard Fässler, Deane F. Mosher

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


β1-null GD25 fibroblasts adherent to vitronectin fail to bind the N- terminal 70-kDa matrix assembly domain of fibronectin or to assemble fibronectin (Sakai, T., Zhang, Q., Fassler, R., and Mosher, D. F. (1998) J. Cell Biol. 141, 527-538). We have made four observations that extend this finding. First, the presence of vitronectin on a substrate that otherwise can support fibronectin assembly has a dominant-negative effect on assembly. Second, the dominant-negative effect is lost when active β1A is expressed. Third, β1A containing the extracellular D130A inactivating mutation has a dominant-negative effect on fibronectin assembly. Fourth, β1-null cells adherent to vitronectin are fiat and lack filopodia, whereas β1-null cells adherent to fibronectin or β1A-expressing cells adherent to either vitronectin or fibronectin are contracted and exhibit numerous filopodia. These results reveal, therefore, that GD25 cells adherent to vitronectin can only assume a shape suitable for assembly of fibronectin when there is a countervailing signal from functional β1-integrins.

Original languageEnglish
Pages (from-to)368-375
Number of pages8
JournalJournal of Biological Chemistry
Issue number1
Publication statusPublished - 01-01-1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Functional β1-integrins release the suppression of fibronectin matrix assembly by vitronectin'. Together they form a unique fingerprint.

Cite this