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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.

Original publication

DOI

10.1074/jbc.m709327200

Type

Journal article

Journal

The Journal of biological chemistry

Publication Date

05/2008

Volume

283

Pages

13053 - 13062

Addresses

Department of Matrix Biology, Imperial College London, Hammersmith, London W6 8LH, UK. y.itoh@imperial.ac.uk

Keywords

Cell Line, Cell Membrane, Animals, Cercopithecus aethiops, Mice, Collagen, Protein Precursors, Enzyme Activation, Amino Acid Sequence, Amino Acid Motifs, Protein Structure, Tertiary, Dimerization, Solubility, Molecular Sequence Data, Matrix Metalloproteinase 2, Matrix Metalloproteinase 14