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Papers In Press, published online ahead of print November 27, 2001
J. Biol. Chem, 10.1074/jbc.M110269200
Submitted on October 25, 2001
Revised on November 14, 2001
Accepted on November 23, 2001

Processing of integrin alphaV subunit by MT1-MMP stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of FAK

Elena I. Deryugina, Boris I. Ratnikov, Tanya I. Postnova, Dmitri V. Rozanov, and Alex Y. Strongin

N/A, The Burnham Institute, La Jolla, CA 92037

Corresponding Author: strongin{at}burnham.org

Recently, we have shown that membrane type-1 matrix metalloproteinase (MT1-MMP) exhibits integrin convertase activity. Similarly to furin-like proprotein convertases (PC), MT1-MMP directly processes a single chain precursor of alphaV integrin subunit (pro-alphaV) into the heavy and light alpha-chains connected by a disulfide bridge. To evaluate functionality of MT1-MMP-processed integrins, we examined breast carcinoma MCF7 cells co-expressing alphaVbeta3 integrin with either the wild type or mutant MT1-MMP in a variety of migration and adhesion tests. Specific inhibitors of PC and MMP were employed in our cell system to attenuate the individual pathways of pro-alphaV maturation. Here, we present evidence that MT1-MMP cleavage of pro-alphaV in the cells did not affect RGD-ligand binding of the resulting alphaVbeta3 integrin but enhanced outside-in signal transduction through a focal adhesion kinase (FAK) pathway. Enhanced tyrosine phosphorylation of FAK in cells co-expressing MT1-MMP and alphaVbeta3 integrin contributed to efficient adhesion and especially, migration of cells on vitronectin, a ligand of alphaVbeta3 integrin. These mechanisms underscore significance of a coordinated interplay between MT1-MMP and alphaVbeta3 integrin in tumor cells, and identify downstream signaling pathway resulting from their interactions. Regulation of integrin maturation and functionality may be an important role of MT1-MMP in tumor cells.


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