The tetraspanin network modulates MT1-MMP cell surface trafficking
The membrane-type 1 matrix metalloproteinase (MT1-MMP) drives fundamental physiological and pathophysiological processes. Among other substrates, MT1-MMP cleaves components of the extracellular matrix and activates other matrix-cleaving proteases such as MMP-2. Trafficking is a highly effective mean...
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| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 March 2013
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| In: |
International journal of biochemistry & cell biology
Year: 2013, Jahrgang: 45, Heft: 6, Pages: 1133-1144 |
| ISSN: | 1878-5875 |
| DOI: | 10.1016/j.biocel.2013.02.020 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.biocel.2013.02.020 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S1357272513000678 
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| Verfasserangaben: | H.M. Schröder, S.C. Hoffmann, M. Hecker, T. Korff, T. Ludwig |
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| 245 | 1 | 4 | |a The tetraspanin network modulates MT1-MMP cell surface trafficking |c H.M. Schröder, S.C. Hoffmann, M. Hecker, T. Korff, T. Ludwig |
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| 520 | |a The membrane-type 1 matrix metalloproteinase (MT1-MMP) drives fundamental physiological and pathophysiological processes. Among other substrates, MT1-MMP cleaves components of the extracellular matrix and activates other matrix-cleaving proteases such as MMP-2. Trafficking is a highly effective means to modulate MT1-MMP cell surface expression, and hence regulate its function. Here, we describe the complex interaction of MT1-MMP with tetraspanins, their effects on MT1-MMP intracellular trafficking and proteolytic function. Tetraspanins are credited as membrane organizers that form a network within the membrane to regulate the trafficking of associated proteins. In short, we found MT1-MMP to interact with the tetraspanin-associated EWI-2 protein by a yeast two-hybrid screen. Immunoprecipitation analysis confirmed this interaction and further revealed that MT1-MMP also stably interacts with distinct tetraspanins (CD9, CD37, CD53, CD63, CD81, and CD82) and the tetraspanin-like MAL protein. By using different MT1-MMP truncation constructs and mutants, we observed that all tetraspanins and MAL associated with the hemopexin domain of MT1-MMP. Moreover, this interaction was independent of O-glycosylation of MT1-MMP and exclusively occurred in the endoplasmic reticulum. Here, the respective subcellular compartment was identified by fitting the MT1-MMP interaction pattern to a model for post-translational processing of MT1-MMP. In addition, tetraspanins differentially affected the cell surface localization of MT1-MMP, its capacity to activate pro-MMP-2, and the collagen invasion capacity. Interestingly, the degree of tetraspanin-MT1-MMP association did not correlate with its impact on MT1-MMP function. Tetraspanins thus distinctly affect MT1-MMP subcellular localization and function, and may constitute an effective mechanism to control MT1-MMP-dependent proteolysis at the cell surface. | ||
| 650 | 4 | |a Cancer | |
| 650 | 4 | |a Cell surface trafficking | |
| 650 | 4 | |a MT1-MMP | |
| 650 | 4 | |a Protein-protein interaction | |
| 650 | 4 | |a Tetraspanin | |
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| 700 | 1 | |a Ludwig, Thomas |e VerfasserIn |0 (DE-588)1149075333 |0 (DE-627)1009355244 |0 (DE-576)496538217 |4 aut | |
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