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Cellular and molecular mechanisms of MT1-MMP-dependent cancer cell invasion.
Abstract
Metastasis is responsible for most cancer-associated deaths. Accumulating evidence based on 3D migration models has revealed a diversity of invasive migratory schemes reflecting the plasticity of tumor cells to switch between proteolytic and nonproteolytic modes of invasion. Yet, initial stages of localized regional tumor dissemination require proteolytic remodeling of the extracellular matrix to overcome tissue barriers. Recent data indicate that surface-exposed membrane type 1–matrix metalloproteinase (MT1-MMP), belonging to a group of membrane-anchored MMPs, plays a central role in pericellular matrix degradation during basement membrane and interstitial tissue transmigration programs. In addition, a large body of work indicates that MT1-MMP is targeted to specialized actin-rich cell protrusions termed invadopodia, which are responsible for matrix degradation. This review describes the multistep assembly of actin-based invadopodia in molecular details. Mechanisms underlying MT1-MMP traffic to invadopodia through endocytosis/recycling cycles, which are key to the invasive program of carcinoma cells, are discussed.
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The catalytic domain is highly conserved among MMP family members.
“The catalytic domain is highly conserved among MMP family members (19, 24).”
From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [24]
The cytoplasmic tail of MT1-MMP plays an important role in endocytosis of MT1-MMP and the localization of MT1-MMP on specific microdomains in the plasma membrane.
“The cytoplasmic tail of MT1-MMP plays an important role in endocytosis of MT1-MMP and the localization of MT1-MMP on the specific microdomains in the plasma membrane (19, 23–25).”
From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [24]
Physiologically, MMP14 cleaves a wide range of substrates, ranging from ECM to growth factor receptors, in a tissue-specific and contextual manner.
“Physiologically, MMP14 cleaves a wide range of substrates, ranging from ECM to growth factor receptors, in a tissue-specific and contextual manner13,14.”
From MT1-MMP inhibition rejuvenates ageing brain and rescues cognitive deficits in obesity (2025) · cites this paper as [14]
Citations
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Diaz, B., Shani, G., Pass, I., Anderson, D., Quintavalle, M., & Courtneidge, S. A. (2009) · Science Signaling · doi:10.1126/scisignal.2000368 · Cited by 242
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Metadata
- Authors
- Castro-Castro, A., Marchesin, V., Monteiro, P., Lodillinsky, C., Rossé, C., & Chavrier, P.
- Affiliations
- Cell Polarity, Migration and Cancer Unit, Institut Pasteur, Paris, F-75724 France
- Imagine Institute of Genetic Diseases, Paris, F-75015 France
- Barts Cancer Institute, University of London John Vane Science Centre, London EC1M 6BQ, United Kingdom
- Instituto de Oncologia Ángel H. Roffo, Research Area, Buenos Aires, C1417DTB, Argentina
- Institut Curie, Paris, F-75248 France;
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2016-10-06
- Volume
- 32
- Issue
- 1
- Pages
- 555-576
- ISSN
- 1081-0706
- 1530-8995
- Cited by
- 249
- References
- 3
- Language
- en
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