2026-06-14T03:28:57Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/92442024-09-27T08:54:27Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605col_20.500.12105_19607
Repisalud
author
Suárez, Henar
author
López-Martín, Soraya
author
Toribio, Victor
author
Zamai, Moreno
author
Hernandez-Riquer, Maria Victoria
author
Genis, Laura
author
Arroyo, Alicia G
author
Yanez-Mo, Maria
funder
Ministerio de Economía y Competitividad (España)
funder
Fundación Ramón Areces
funder
Instituto de Salud Carlos III
funder
Fundación ProCNIC
funder
Ministerio de Ciencia, Innovación y Universidades (España)
funder
Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
2020-03-09T13:18:56Z
2020-03-09T13:18:56Z
2020-02
Cells. 2020; 9(2):348
10.3390/cells9020348
2073-4409
2073-4409
Cells
32028690
http://hdl.handle.net/20.500.12105/9244
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.
eng
ERM
MT1-MMP
Extracellular vesicles
Tetraspanin enriched-microdomains
Regulation of MT1-MMP Activity through Its Association with ERMs
journal article
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