Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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

J biol chem

Publication Date

09/05/2008

Volume

283

Pages

13053 - 13062

Keywords

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