The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.
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 tran...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2008
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| _version_ | 1826288246637723648 |
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| author | Itoh, Y Ito, N Nagase, H Seiki, M |
| author_facet | Itoh, Y Ito, N Nagase, H Seiki, M |
| author_sort | Itoh, Y |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T02:10:49Z |
| format | Journal article |
| id | oxford-uuid:a0949296-d654-4825-85f3-a48770b569ae |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:10:49Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:a0949296-d654-4825-85f3-a48770b569ae2022-03-27T02:06:27ZThe second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:a0949296-d654-4825-85f3-a48770b569aeEnglishSymplectic Elements at Oxford2008Itoh, YIto, NNagase, HSeiki, MActivation 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. |
| spellingShingle | Itoh, Y Ito, N Nagase, H Seiki, M The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title | The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title_full | The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title_fullStr | The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title_full_unstemmed | The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title_short | The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface. |
| title_sort | second dimer interface of mt1 mmp the transmembrane domain is essential for prommp 2 activation on the cell surface |
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