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MBC in Press, published online ahead of print May 21, 2008
Mol. Biol. Cell 10.1091/mbc.E08-01-0016

A more recent version of this article appeared on August 1, 2008
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Submitted on January 9, 2008
Revised on May 6, 2008
Accepted on May 12, 2008

Molecular Dissection of the Structural Machinery Underlying the Tissue-Invasive Activity of MT1-MMP

Xiao-Yan Li, Ichiro Ota, Ikuo Yana, Farideh Sabeh, and Stephen J. Weiss

Division of Molecular Medicine and Genetics, Department of Internal Medicine, The Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109

Monitoring Editor: Mark H. Ginsberg

Membrane type-I matrix metalloproteinase (MT1-MMP) drives cell invasion through three-dimensional (3-D) extracellular matrix (ECM) barriers dominated by type I collagen or fibrin. Based largely on analyses of its impact on cell function under 2-D culture conditions, MT1-MMP is categorized as a multifunctional molecule with i) a structurally distinct, N-terminal catalytic domain ii) a C-terminal hemopexin domain that regulates substrate recognition as well as conformation and iii) a type I transmembrane domain whose cytosolic tail controls protease trafficking and signaling cascades. The MT1-MMP domains that subserve cell trafficking through 3-D ECM barriers in vitro or in vivo, however, remain largely undefined. Herein, we demonstrate that collagen-invasive activity is not confined strictly to the catalytic, hemopexin, transmembrane or cytosolic domain sequences of MT1-MMP. Indeed, even a secreted collagenase supports invasion when tethered to the cell surface in the absence of the MT1-MMP hemopexin, transmembrane and cytosolic tail domains. By contrast, the ability of MT1-MMP to support fibrin-invasive activity diverges from collagenolytic potential, and alternatively requires the specific participation of MT-MMP catalytic and hemopexin domains. Hence, the tissue-invasive properties of MT1-MMP are unexpectedly embedded within distinct, but parsimonious, sequences that serve to tether the requisite matrix-degradative activity to the surface of migrating cells.

Address correspondence to: Stephen J. Weiss (sjweiss{at}umich.edu)




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