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J. Biol. Chem., Vol. 283, Issue 19, 13053-13062, May 9, 2008

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The Second Dimer Interface of MT1-MMP, the Transmembrane Domain, Is Essential for ProMMP-2 Activation on the Cell Surface^*

Yoshifumi Itoh¹, Noriko Ito, Hideaki Nagase, and Motoharu Seiki

From the Department of Matrix Biology, Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 65 Aspenlea Road, Hammersmith, London W6 8LH, United Kingdom and the Division of Cancer Cell Research, Institute of Medical Science, The University of Tokyo, 4-6-1 Minatoku, Tokyo 108-8639, Japan

Activation of proMMP-2 and cell surface collagenolysis are important activities of membrane-type 1 matrix metalloproteinase (MT1-MMP) to promote cell migration in tissue, and these activities are regulated by homodimerization of MT1-MMP on the cell surface. In this study, we have identified the transmembrane domain as a second dimer interface of MT1-MMP in addition to the previously identified hemopexin domain. Our analyses indicate that these two modes of dimerization have different roles; transmembrane-dependent dimerization is critical for proMMP-2 activation, whereas hemopexin-dependent dimerization is important for degradation of collagen on the cell surface. Our finding provides new insight into the potential molecular arrangement of MT1-MMP contributing to its function on the cell surface.

Received for publication, November 13, 2007 , and in revised form, February 21, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grant AR40994. This work was also supported by Cancer Research UK Project Grant C1507/A5541 and the Wellcome Trust equipment grant, and the Arthritis Research Campaign core grant to the Kennedy Institute of Rheumatology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Fax: 44-20-8383-4760; E-mail: y.itoh{at}imperial.ac.uk.

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