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Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells.

Rozanov, Dmitri V, Deryugina, Elena I, Monosov, Edward Z, Marchenko, Natalia D, Strongin, Alex Y·2004·Experimental Cell Research

Abstract

Membrane type-1 matrix metalloproteinase (MT1-MMP) is a key enzyme in cell locomotion and tissue remodeling. Trafficking to the plasma membrane and internalization into the transient storage compartment both regulate the cell surface presentation of MT1-MMP. Our data indicate that mutant MT1-MMP lacking the cytoplasmic tail is recruited to the caveolae-enriched lipid raft membrane microdomains in breast carcinoma MCF7 cells. In contrast, the wild-type protease is not permanently associated with lipid rafts. Trafficking to lipid rafts correlated with poor internalization and the persistent presentation of MT1-MMP at the cell surface. The tail mutant efficiently functioned in inducing the activation of the latent proMMP-2 zymogen, matrix remodeling, and contraction of three-dimensional collagen lattices. Recruitment of the tail mutant to lipid raft antagonized, however, the cleavage of the plasma membrane-associated E-cadherin. These events limited the contribution of the tail mutant to cell locomotion and malignant growth. It is conceivable that the tail peptide sequence plays a crucial role in the translocations of MT1-MMP across the cell and contributes to coordinated cellular functions. It is tempting to hypothesize that the mechanisms involved in trafficking of MT1-MMP to caveolin-enriched lipid rafts may be targeted in a clinically advantageous manner.

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Crossref · 10.1016/j.yexcr.2003.10.006

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  • Deletion of the cytoplasmic tail did not affect the trafficking of MT1-MMP to the plasma membrane nor its ability to activate proMMP2, but the mutant proteins displayed a different distribution pattern on the cell surface and an impaired ability to mediate cell invasion compared to the wild-type protein.

    “Deletion of the cytoplasmic tail did not affect the trafficking of MT1-MMP to the plasma membrane nor its ability to activate proMMP2, but the mutant proteins displayed a different distribution pattern on the cell surface and an impaired ability to mediate cell invasion compared to the wild-type protein (59, 60).”

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Metadata

Authors
Rozanov, D. V., Deryugina, E. I., Monosov, E. Z., Marchenko, N. D., & Strongin, A. Y.
Venue
Experimental Cell Research
Publisher
Elsevier BV
Published
2004-02
Volume
293
Issue
1
Pages
81-95
ISSN
0014-4827
Cited by
64
References
1
Language
en

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