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The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.

Abstract:

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; t...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m709327200

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDORMS
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDORMS
Role:
Author
Journal:
Journal of biological chemistry
Volume:
283
Issue:
19
Pages:
13053-13062
Publication date:
2008-05-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
224631

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