Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MaTAR25 lncRNA regulates the Tensin1 gene to impact breast cancer progression

ABSTRACT: Misregulation of long non-coding RNA genes has been linked to a wide variety of cancer types. Here we report on Mammary Tumor Associated RNA 25 (MaTAR25), a nuclear enriched and chromatin associated lncRNA that plays a role in mammary tumor cell proliferation, migration, and invasion, both in vitro and in vivo. MaTAR25 functions by interacting with purine rich element binding protein B, and associating with a major downstream target gene Tensin 1 (Tns1) to regulate its expression in trans. Knockout of MaTAR25 results in down-regulation of Tns1 leading to a reorganization of the actin cytoskeleton, and a reduction of focal adhesions and microvilli. The human ortholog of MaTAR25, LINC01271, is upregulated with human breast cancer stage and metastasis.

ORGANISM(S): Mus musculus

PROVIDER: GSE142169 | GEO | 2020/10/19

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

Project description:Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signaling. However, the function of tensin-2 beyond localizing to focal adhesions remain poorly understood. We utilized proximity-dependent biotinylation and strep-tag affinity proteomics to identify interaction partners of tensin-2 in HEK293 cells. Interactomics linked tensin-2 to known focal adhesion proteins and the dystrophin glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in HEK293 and MEF cells and found that pY483 tensin-2 is enriched in adhesions in MEF cells. Our study unveils novel interaction partners for tensin-2 and further solidifies its speculated role in cell energy metabolism. These findings shed fresh insight on the functions of tensin-2, highlighting its potential as a therapeutic target for diseases associated with impaired cell adhesion and metabolism.

2024-07-20 | GSE231782 | GEO

Development and Characterization of an Inducible Tensin1 Deficient Transgenic Murine Model

Project description:Tensin1 (TNS1) is a key component of focal and fibrillar adhesions, mediating fibrillogenesis, as well as the transduction of mechanical cues and adhesive signaling. To enable further TNS1 characterization, we have developed a novel transgenic mouse that allows for temporally controlled and lineage specific knockout of TNS1. We found no differentially observed effects of TNS1 knockout on mouse health, breeding capacity, or vital organ histopathology. In contrast, RNA sequencing analysis identified 171 differentially expressed genes with Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis demonstrating differential expression in osteoclast differentiation and a number of pathways involved in host immune response. Furthermore, STRING pathway analysis showed differential regulation of genes involved in B-cell and myeloid-related signaling pathways, a number of which were validated by reverse transcription-quantitative polymerase chain reaction (RT qPCR). These findings were corroborated by impaired function of TNS1 siRNA monocytes and increased detection of lymphocytes in the bronchoalveolar lavage within days following TNS1 knockout. This study provides a novel understanding of the phenotypic and genotypic changes that occur following knockout of TNS1 that may lead to subsequent understanding of its role in disease.

2026-02-14 | GSE319060 | GEO

Tensin 2 interactomics reveals interaction with GAPDH and a phosphorylation-mediated regulatory role in glycolysis

Project description:Integrin adaptor proteins, like tensin-2, are crucial for cell adhesion and signalling. However, its functions beyond localizing to focal adhesions remain poorly understood. To identify tensin-2's interaction partners in HEK293 cells, we utilized proximity-dependent biotinylation and strep-tag affinity proteomics. Results linked tensin-2 to known focal adhesion proteins and the dystrophin-glycoprotein complex, while also uncovering novel interaction with the glycolytic enzyme GAPDH. We demonstrated that Y483-phosphorylation of tensin-2 regulates the glycolytic rate in HEK293 and MEF cells, as well as gene expression in HEK293 cells. Of note, Y483-phosphorylation directs tensin-2 to adhesion sites in MEF cells. Our study unveils numerous novel interaction partners for tensin-2, further solidifies its speculated role in cell energy metabolism and identifies Y483-phosphorylation as a crucial regulator for tensin-2 localization. These findings shed fresh insight into the functions of tensin-2, highlighting its potential as a therapeutic target for diseases associated with impaired cell adhesion and metabolism.

2023-05-02 | MSV000091836 | MassIVE

GFAT1 promotes the progression of hepatocellular carcinoma via enhancing the O-GlcNAcylation of VEZF1 [RNA-seq]

Project description:Glutamine-fructose-6-phosphate amidotransferase 1 (GFAT1), the first rate-limiting enzyme in the hexosamine biosynthetic pathway (HBP), is a key factor controlling HBP flux. However, the molecular mechanism underlying the roles of GFAT1 in hepatocellular carcinoma (HCC) remain to be elucidated. Here, we found that GFAT1 was upregulated in HCC, and high GFAT1 level was correlated with poor patient prognosis. Our in vitro and in vivo studies demonstrated that GFAT1 facilitated hepatoma cell proliferation and invasion by enhancing HBP and O-GlcNAcylation through its enzymatic activity. Global profiling of O-GlcNAcylation identified vascular endothelial zinc finger protein 1 (VEZF1) as a substrate heavily O-GlcNAcylated in GFAT1-overexpressing hepatoma cells. Notably, O-GlcNAcylation at specific serine residues (Ser123 and Ser124) within VEZF1 attenuated its proteasomal degradation, thereby enhancing its protein stability and promoting tensin 1 (TNS1) transcription in HCC. In addition, we designed a bioactive VEZF1-derived peptide to competitively inhibit GFAT1-mediated O-GlcNAcylation of VEZF1. This intervention effectively reduced TNS1 expression and suppressed the progression of HCC in a mouse model. Together, these findings highlight the therapeutic potential of targeting the GFAT1-VEZF1-TNS1 signaling axis in HCC.

2025-08-26 | GSE278334 | GEO

GFAT1 promotes the progression of hepatocellular carcinoma via enhancing the O-GlcNAcylation of VEZF1

2025-08-26 | GSE278232 | GEO

The quantitative proteomics analysis of TGF-β induced EMT in A549 cells and TNS-overexpressing A549 cells

Project description:Metastasis is the primary cause of mortality in lung cancer patients, with the epithelial-mesenchymal transition (EMT) process conferring increased metastatic potential to carcinoma cells. While emerging evidence suggests that TNS1 contributes to carcinoma metastasis, it remains unclear the role of TNS1 in EMT. In this study, we reveal TNS1 as an indispensable factor in TGF-β and hypoxia mediated EMT process. Elevated TNS1 protein levels are closely correlated with a worse prognosis in lung cancer patients. TNS1 is also found to potently promote EMT process and tumor metastasis in vitro and in vivo. Mechanistically, TNS1 expression is mediated by the transcription factor SMAD3 in TGF-β signaling. Moreover, TNS1 interacts with and modulates ZEB1 expression, preventing ZEB1 ubiquitination degradation. Therefore, our study reveals the role of TNS1 in the EMT process and suggests that TNS1 promises to a candidate for targeted cancer therapy.

2025-12-08 | PXD057161 | Pride

In Situ Structure of Intestinal Apical Surface Reveals Nanovilli on Microvilli

Project description:Microvilli are actin bundle-supported membrane protrusions essential for absorption, secretion, and sensation. Microvilli defects cause human diseases, including gastrointestinal disorders and inherited deafness; however, mechanisms controlling microvilli formation and organization remain unclear. Here, we study microvilli by vitrifying the C. elegans larvae and mouse intestinal tissues with high-pressure freezing, thinning them by cryo-focused ion beam milling, cryo-electron tomography, and sub-tomogram averaging. We show that hundreds of previously unrecognized stick-like structures, which we refer to as nanovilli, decorate the lateral surface of C. elegans and mouse microvilli. The C. elegans 37.5-nm long and 4.5-nm wide nanovilli are composed of the protocadherin family protein CDH-8. Loss of nanovilli slows down animal growth and increases the number of Y-shaped microvilli, intermediate structures when a microvillus splits from its tip and separates into two. Our results indicate that nanovilli space microvilli and suggest a microvilli division model through which microvilli assemble with striking uniformity.

2021-04-30 | GSE167859 | GEO

Capture of TAD reorganization endows variant patterns of gene transcription (RNA-Seq)

Project description:TAD (Topologically Associating Domain) reorganization occurs commonly in cell nucleus and contributes to gene activation and inhibition through separation or fusion of adjacent TADs. However, identification of functional genes impacted by TAD alteration and revealing of TAD-reorganization mechanism underlying gene transcription remain to be fully elucidated. Here, we firstly developed a novel approach termed Inter3D to specifically dig out genes regulated by TAD reorganization. By constructing the comprehensive TAD reorganization medicating epigenomic landscapes in tumor cells, we showed that TAD separation interrupted the intrachromosomal loop at MYL12B locus and abrogated its transcription, while TAD fusion generated the chromosomal interaction and triggered CYP27B1 activation. Our study provides a comprehensive insight into capture of TAD rearrangement-mediated gene loci and moves towards recognizing the functional role of TAD reorganization in gene transcription.

2024-04-29 | GSE230797 | GEO