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Regulation of MT1-MMP Activity through Its Association with ERMs

Molecular Biology Department, Universidad Autónoma de Madrid (UAM), 28049 Madrid, Spain
Severo Ochoa Molecular Biology Center (CBM-SO), Instituto de Investigación Sanitaria Princesa (IIS-IP), 28049 Madrid, Spain
Unit of Microscopy and Dynamic Imaging, Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain
Vascular Pathophysiology Department, Centro Nacional de Investigaciones Cardiovasculares (CNIC), 28029 Madrid, Spain
Molecular Biomedicine Department, Centro de Investigaciones Biológicas Margarita Salas (CIB-CSIC), 28040 Madrid, Spain
Author to whom correspondence should be addressed.
Cells 2020, 9(2), 348;
Received: 17 December 2019 / Revised: 31 January 2020 / Accepted: 1 February 2020 / Published: 3 February 2020
(This article belongs to the Special Issue Extracellular Matrix Remodeling 2019)
Membrane-bound proteases play a key role in biology by degrading matrix proteins or shedding adhesion receptors. MT1-MMP metalloproteinase is critical during cancer invasion, angiogenesis, and development. MT1-MMP activity is strictly regulated by internalization, recycling, autoprocessing but also through its incorporation into tetraspanin-enriched microdomains (TEMs), into invadopodia, or by its secretion on extracellular vesicles (EVs). We identified a juxtamembrane positively charged cluster responsible for the interaction of MT1-MMP with ERM (ezrin/radixin/moesin) cytoskeletal connectors in breast carcinoma cells. Linkage to ERMs regulates MT1-MMP subcellular distribution and internalization, but not its incorporation into extracellular vesicles. MT1-MMP association to ERMs and insertion into TEMs are independent phenomena, so that mutation of the ERM-binding motif in the cytoplasmic region of MT1-MMP does not preclude its association with the tetraspanin CD151, but impairs the accumulation and coalescence of CD151/MT1-MMP complexes at actin-rich structures. Conversely, gene deletion of CD151 does not impact on MT1-MMP colocalization with ERM molecules. At the plasma membrane MT1-MMP autoprocessing is severely dependent on ERM association and seems to be the dominant regulator of the enzyme collagenolytic activity. This newly characterized MT1-MMP/ERM association can thus be of relevance for tumor cell invasion. View Full-Text
Keywords: MT1-MMP; ERM; tetraspanin enriched-microdomains; extracellular vesicles MT1-MMP; ERM; tetraspanin enriched-microdomains; extracellular vesicles
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MDPI and ACS Style

Suárez, H.; López-Martín, S.; Toribio, V.; Zamai, M.; Hernández-Riquer, M.V.; Genís, L.; Arroyo, A.G.; Yáñez-Mó, M. Regulation of MT1-MMP Activity through Its Association with ERMs. Cells 2020, 9, 348.

AMA Style

Suárez H, López-Martín S, Toribio V, Zamai M, Hernández-Riquer MV, Genís L, Arroyo AG, Yáñez-Mó M. Regulation of MT1-MMP Activity through Its Association with ERMs. Cells. 2020; 9(2):348.

Chicago/Turabian Style

Suárez, Henar, Soraya López-Martín, Víctor Toribio, Moreno Zamai, M. Victoria Hernández-Riquer, Laura Genís, Alicia G. Arroyo, and María Yáñez-Mó. 2020. "Regulation of MT1-MMP Activity through Its Association with ERMs" Cells 9, no. 2: 348.

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