Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Macroscopic mechanostress-induced nuclear envelope rupture reorganizes tumor–stromal interactions in plantar melanoma

ABSTRACT: To delineate transcriptome changes associated with nuclear envelope rupture, B16F10 cells were transfected with either control siRNA or Ndc1 siRNAs. Cells were harvested 48 hr post-transfection and subjected to RNA-sequencing analysis.

ORGANISM(S): Mus musculus

PROVIDER: GSE312609 | GEO | 2026/09/01

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Macroscopic mechanostress-induced nuclear envelope rupture reorganizes tumor–stromal interactions in plantar melanoma

Project description:Macroscopic mechanostress-induced nuclear envelope rupture reorganizes tumor–stromal interactions in plantar melanoma

| PRJNA1375538 | ENA

Macroscopic mechanostress-induced nuclear envelop rupture reorganizes tumor-stromal interactions (scRNA-seq)

Project description:Macroscopic mechanostress can disrupt nuclear envelop integrity of cancer cell. However, the impact of this stimuli on the tumor microenvironment remians unclear. Here, by constructing a single-cell RNA sequencing data of hindpaw-engrafted B16F10 melanoma with/without forced wheel running, we show that reorganization of fibroblast and macrophage subtypes. Fibroblasts from running group showed upregulated Acta2 and Lrrc15 expression with increased ECM production. IL-1b expressing macrophage subtype proportion was increased in running group. Collectively, these data elucidate the changes within the tumor microenvironment upon macroscopic mechanostress.

2026-06-01 | GSE289587 | GEO

Nuclear envelope rupture causes RNA polymerase loss in LMNA cardiomyopathy

Project description:Localized rupture of the nuclear envelope has been reported in various pathologies, including cancer, neurodegenerative disease, myocardial infarction, as well as dilated cardiomyopathy caused by Lamin A/C gene mutations (LMNA-DCM). Whether and how nuclear rupture contributes to disease remains unclear. Here, we report that nuclear rupture causes global transcriptional deficiency in a mouse model of LMNA-DCM. We observed that ruptured nuclei lost chromatin-bound RNA polymerase II, leading to downregulation of numerous genes essential for cardiomyocyte structure and function. Notably, over one third of ruptured nuclei resealed and regained transcription. Resealing involved the ESCRT-III membrane remodeling complex and was cardioprotective, as its blockade increased rupture frequency and accelerated cardiomyopathy. However, resealing was ineffective: resealed nuclei re-ruptured at twice the resealing rate and ten-fold faster than the de novo rupture rate. A mathematical model predicted a steady accumulation of ruptured nuclei despite ongoing resealing. Consistently, a human LMNA-mutant heart contained numerous ruptured nuclei at the time of disease presentation. These findings link nuclear rupture to organ deterioration through global transcriptional deficiency and suggested rupture repair as a critical modifier of nuclear rupture-associated conditions.

2026-04-03 | GSE325163 | GEO

Nuclear envelope rupture causes RNA polymerase loss in LMNA cardiomyopathy

Project description:Nuclear envelope rupture causes RNA polymerase loss in LMNA cardiomyopathy

| PRJNA1438739 | ENA

Macroscopic mechanostress-induced nuclear envelop rupture reorganizes tumor-stromal interactions (scRNA-seq)

Project description:Macroscopic mechanostress-induced nuclear envelop rupture reorganizes tumor-stromal interactions (scRNA-seq)

| PRJNA1223475 | ENA

Actin polymerization by WASp limits nuclear envelope rupture and inflammation in macrophages

Project description:Actin polymerization by WASp limits nuclear envelope rupture and inflammation in macrophages

| PRJNA1201051 | ENA

DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of Lamin A/C

Project description:The integrity of the nuclear envelope (NE) is essential to maintain the structural stability of the nucleus. Rupture of the NE has been frequently observed in cancer cells, especially in the context of mechanical challenges, such as physical confinement and migration. However, spontaneous NE rupture events have also been described, without any obvious physical challenges to the cell. The molecular mechanism(s) of these spontaneous NE rupture events remain to be explored. Here, we show that DNA damage and subsequent ATR activation can lead to NE rupture. Upon DNA damage, Lamin A/C is phosphorylated in an ATR-dependent manner, leading to changes in lamina assembly and, ultimately, NE rupture. In addition, we show that cancer cells with intrinsic DNA repair defects undergo frequent events of DNA damage-induced NE rupture, which renders them extremely sensitive to further NE perturbations. Exploiting this NE vulnerability could provide a new angle to complement traditional, DNA damage-based chemotherapy.

2023-10-09 | PXD040857 | Pride

DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of Lamin A/C - Synthetic Peptide

2023-10-09 | PXD043990 | Pride

Actin polymerization by WASp limits nuclear envelope rupture and inflammation in macrophages I

Project description:Actin polymerization by WASp limits nuclear envelope rupture and inflammation in macrophages I

| PRJNA1201748 | ENA

Targeting of Tumor Cells by the Adenovirus E4orf4 protein via Par3 Polarity Protein-Regulated Nuclear Envelope Rupture

Project description:The protein product of the Early region 4 open reading frame 4 (E4orf4) of human adenovirus 2 is reported to exhibit a tumor-selective cell killing activity. Here, we show that E4orf4’s tumoricidal activity correlated with changes in perinuclear actomyosin contractility that are controlled by an interaction with the Par3 polarity protein. Surprisingly, E4orf4 enhanced apical-basal polarity in non-transformed mammary epithelial cells. In contrast, in tumorigenic cells, it induced a high incidence of actin-dependent nuclear bleb rupture. This process, which was regulated by the linker of nucleoskeleton and cytoskeleton (LINC) complex, promoted nuclear efflux of E4orf4 and the breakdown of the nuclear compartment. Significantly, Par3 also regulated the incidence of transient nuclear envelope rupture due to the reduced nuclear rigidity in cells depleted of lamins, in absence of E4orf4. Thus, using E4orf4 as a probing tool, we uncovered a so far un-appreciated role for Par3 in controlling the actin-dependent forces acting on the nuclear envelope to remodel nuclear shape, which might be a defining feature of tumor cells that is harnessed by E4orf4.

2020-03-19 | PXD014329 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data