Moesin regulates the motility of oral cancer cells via MT1-MMP and E-cadherin/p120-catenin adhesion complex

Li, Yao-yin; Zhou, Chuan‐Xiang; Gao, Yan

doi:10.1016/j.oraloncology.2015.07.003

Cited by 23 publications

(35 citation statements)

References 32 publications

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“…Since the dynamics of MT1-MMP turnover and insertion into the plasma membrane are critical for its pro-invasive actions [24], the increased activity of MT1-MMP in the absence of ERM association will probably directly impact also in a 3D scenario in tumour cell invasion. It has been recently reported that moesin knock-down impacts on MT1-MMP expression levels in oral cancer cells [56]. In this report, however, the autoprocessing of the protease or its direct interaction with moesin was not.…”

Section: Discussioncontrasting

confidence: 65%

“…ERM molecules interact with a wide variety of cell surface proteins and receptors, such as CD44 [52], ICAM3 [53] or tetraspanins [54] creating specialized signalling platforms [55]. Previous reports have shown some evidence that relate moesin with MT1-MMP expression levels in tumour cells [56], however, the molecular mechanisms involved are unknown.…”

Section: Introductionmentioning

confidence: 99%

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Regulation of MT1-MMP Activity through Its Association with ERMs

Suárez

López-Martín

Toribio

et al. 2020

Cells

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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.

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Section: Discussioncontrasting

confidence: 65%

Section: Introductionmentioning

confidence: 99%

Regulation of MT1-MMP Activity through Its Association with ERMs

Suárez

López-Martín

Toribio

et al. 2020

Cells

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“…All OSCC cells used in the functional assays were transfected with the indicated plasmids and stable colonies were selected. The functional assays, including proliferation, migration, and invasion assays, and colony formation assays, were performed as described previously [ 2 , 19 ].…”

Section: Methodsmentioning

confidence: 99%

“…Oral squamous cell carcinoma (OSCC) is one of the leading causes of cancer death worldwide, and nearly 50% of patients die from the disease [ 1 ]. Regardless of the therapeutic approach, location, or stage of the disease, >50% of patients experience a relapse [ 2 ]. Cell interactions within the tumor microenvironment are now recognized as a crucial element in tumor progression [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Cancer-associated fibroblasts contribute to oral cancer cells proliferation and metastasis via exosome-mediated paracrine miR-34a-5p

et al. 2018

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BackgroundCancer-associated fibroblasts (CAFs) play an important role in regulating tumor progression by transferring exosomes to neighboring cells. Our aim was to clarify the role of microRNA encapsulated in the exosomes derived from CAFs in oral squamous cell carcinoma (OSCC).MethodsWe examined the microRNA expression profiles of exosomes derived from CAFs and donor-matched normal fibroblasts (NFs) from patients with OSCC. We used confocal microscopy to examine the transportation of exosomal miR-34a-5p between CAFs and OSCC cells. Next, luciferase reporter and its mutant plasmids were used to confirm direct target gene of miR-34a-5p. Phenotypic assays and in vivo tumor growth experiments were used to investigate the functional significance of exosomal miR-34a-5p.FindingsWe found that the expression of miR-34a-5p in CAF-derived exosomes was significantly reduced, and fibroblasts could transfer exosomal miR-34a-5p to OSCC cells. In xenograft experiments, miR-34a-5p overexpression in CAFs could inhibit the tumorigenesis of OSCC cells. We further revealed that miR-34a-5p binds to its direct downstream target AXL to suppress OSCC cell proliferation and metastasis. Stable ectopic expression of AXL in OSCC cells overexpressing miR-34a-5p restored proliferation and motility abolished by the miRNA. The miR-34a-5p/AXL axis promoted OSCC progression via the AKT/GSK-3β/β-catenin signaling pathway, which could induce the epithelial-mesenchymal transition (EMT) to promote cancer cells metastasis. The miR-34a-5p/AXL axis enhanced nuclear translocation of β-catenin and then induced transcriptional upregulation of SNAIL, which in turn activated both MMP-2 and MMP-9.InterpretationThe miR-34a-5p/AXL axis confers aggressiveness in oral cancer cells through the AKT/GSK-3β/β-catenin/Snail signaling cascade and might represent a therapeutic target for OSCC.FundNational Natural Science Foundation of China.

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“…ZEB1 and ZEB2 downregulate the expression of E-cadherin and reduce the adhesion of cells, thus promoting the invasion and metastasis of tumor cells 32-35. MSN, also known as moesin, belongs to ERM family of proteins which appear to function as a cross-linker between membrane proteins and actin-based cytoskeleton 36-39, therefore, it is momentous for recognition between cells, also vital for cell polarity 40, 41. In recent years, lots of evidences indicated that MSN is closely related to initiation and development of tumor 42-44.…”

Section: Introductionmentioning

confidence: 99%

MiR-200c Inhibits the Tumor Progression of Glioma via Targeting Moesin

Qin

Liu

et al. 2017

Theranostics

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We attempt to demonstrate the regulatory role of miR-200c in glioma progression and its mechanisms behind. Here, we show that miR-200c expression was significantly reduced in the glioma tissues compared to paratumor tissues, especially in malignant glioma. Exogenous overexpression of miR-200c inhibited the proliferation and invasion of glioma cells. In addition, the in vivo mouse xenograft model showed that miR-200c inhibited glioma growth and liver metastasis, which is mainly regulated by targeting moesin (MSN). We demonstrated that the expression of MSN in glioma specimens were negatively correlated with miR-200c expression, and MSN overexpression rescued the phenotype about cell proliferation and invasion induced by miR-200c. Moreover, knockdown of MSN was able to mimic the effects induced by miR-200c in glioma cells. These results indicate that miR-200c plays an important role in the regulation of glioma through targeting MSN.

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Moesin regulates the motility of oral cancer cells via MT1-MMP and E-cadherin/p120-catenin adhesion complex

Cited by 23 publications

References 32 publications

Regulation of MT1-MMP Activity through Its Association with ERMs

Regulation of MT1-MMP Activity through Its Association with ERMs

Cancer-associated fibroblasts contribute to oral cancer cells proliferation and metastasis via exosome-mediated paracrine miR-34a-5p

MiR-200c Inhibits the Tumor Progression of Glioma via Targeting Moesin

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