The formation of a fibrillar fibronectin (FN) extracellular matrix requires self-association of FN dimers. In this report, we show that the major sites for self-association are the amino-terminal repeats I1-5 and the first type III repeats. Recombinant FNs and fragments were generated by baculovirus expression of cysteine-rich domains and by bacterial expression of type III repeats as fusion proteins with maltose binding protein. When recombinant polypeptides were immobilized on microtiter wells, FN bound to 70-kDa amino-terminal fragment and to fusion proteins containing repeats III1-2 and III1-6 but not to other type III repeats. Similar results were obtained with a gel overlay assay. Binding was concentration-dependent and saturable. The amino-terminal binding site for III1-2 was further localized to repeats I1-5. Therefore, at least two different sites for FN- FN interaction reside near the amino terminus of the molecule. A model for the regulation of FN matrix assembly is proposed based on intramolecular interactions between these amino-terminal sites.
|Original language||English (US)|
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|State||Published - Nov 11 1994|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology