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First published online May 8, 2008

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Constructing the matrix with PAI1

For cells to migrate and invade, the surrounding extracellular matrix (ECM) must be remodelled, a process that involves both the assembly and proteolysis of ECM components. Plasminogen activator inhibitor 1 (PAI1) is known to slow ECM proteolysis by inhibiting uPA, a protein that (when bound to its cell-surface receptor uPAR) promotes the formation of the protease plasmin. Daniel Vial and Paula McKeown-Longo (p. 1661) now show that PAI1 has another role in matrix assembly. The authors previously demonstrated that PAI1 could stimulate the assembly of the fibronectin matrix, and they now show that this activity is independent of uPA and uPAR but requires the binding of PAI1 to vitronectin. They also show that PAI1 causes the disassembly of β5-integrin-containing focal adhesions, and that the polymerisation of fibronectin can also be stimulated by disrupting the binding of vitronectin to vβ5 integrin. Moreover, β5-integrin-blocking agents increase the number of activated 5β1 integrins at the cell surface. The authors conclude that PAI1 acts by displacing vβ5 integrin from vitronectin, and that this process involves crosstalk between vβ5 and 5β1 integrins. PAI1 has therefore been identified as a novel regulator of the fibronectin matrix.

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Related articles in JCS:

PAI1 stimulates assembly of the fibronectin matrix in osteosarcoma cells through crosstalk between the vβ5 and 5β1 integrins

Daniel Vial and Paula J. McKeown-Longo
JCS 2008 121: 1661-1670. [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 Social Bookmarking                         What's this?