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First published online July 10, 2003

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Making a matrix

The extracellular matrix protein fibronectin has important roles in cell adhesion, migration, growth and differentiation. It is secreted as a soluble dimer but subsequently assembles to form insoluble, multimeric fibrils. The assembly process depends on interactions between fibronectin and cell surface integrins and is regulated by several signalling pathways. In a Commentary on p. 3269, Iwona Wierzbicka-Patynowski and Jean Schwarzbauer discuss work that is shedding light on this complex mechanism. It is usually initiated by binding of 5ß1 integrin to the RGD motif of fibronectin. Since fibronectin is a dimer, this promotes integrin clustering, fibronectin-fibronectin interactions and formation of fibrils. Another consequence of integrin binding is an opening up of the fibronectin molecule to expose hidden multimerization motifs. Recent studies indicate that partial unfolding of the molecule imparts elasticity on fibrils and allows them to remain under tension. This could increase the pliability of the matrix and is probably regulated by signals that control actomyosin contractility. Other signalling molecules that regulate fibronectin assembly include FAK and Src; these tyrosine kinases lie downstream of integrins and appear to participate in feedback loops that target the fibronectin ligand. Indeed perturbation of fibronectin assembly by Src and other oncogene products probably has a significant impact on tumor cell phenotype.

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The ins and outs of fibronectin matrix assembly

Iwona Wierzbicka-Patynowski and Jean E. Schwarzbauer
JCS 2003 116: 3269-3276. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content