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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




Journal article


J biol chem

Publication Date





13053 - 13062


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