Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Nuclear Talin-1 Provides a Bridge Between Cell Adhesion and Gene Expression

ABSTRACT: Talin-1 (TLN1) is best known to activate integrin receptors and transmit mechanical stimuli to the actin cytoskeleton at focal adhesions. However, the localization of TLN1 is not restricted to focal adhesions. By utilizing both subcellular fractionations and confocal microscopy analyses, we show that TLN1 localizes to the nucleus in several human cell lines, where it is tightly associated with the chromatin. Importantly, siRNA-mediated depletion of endogenous TLN1 triggers extensive changes in the gene expression profile of human breast epithelial cells. To determine the functional impact of nuclear TLN1, we expressed a TLN1 fusion protein containing a nuclear localization signal. Our findings revealed that accumulation of nuclear TLN1 alters the expression of a subset of genes and impairs the formation of cell-cell clusters. This study introduces an additional perspective on the canonical view of TLN1 subcellular localization and function.

ORGANISM(S): Homo sapiens

PROVIDER: GSE198191 | GEO | 2025/01/08

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Potential interactors of alpha-tubulin acetyltransferase 1 (αTAT1/MEC17)

Project description:Cell adhesion to the extracellular matrix occurs through integrin-mediated focal adhesions, which sense the mechanical properties of the substrate and impact cellular functions such as cell migration. Mechanotransduction at focal adhesions affects the actomyosin network and contributes to cell migration. Despite being key players in cell adhesion and migration, the role of microtubules in mechanotransduction has been overlooked. Here, we show that substrate rigidity increases microtubule acetylation through β1 integrin signalling in primary rat astrocytes. Moreover, αTAT1, the enzyme responsible for microtubule acetylation, interacts with a major mechanosensing focal adhesion protein, Talin, and is able to tune the distribution of focal adhesions depending on the matrix rigidity. αTAT1 also reorganises the actomyosin network, increases traction force generation and cell migration speed on stiff substrates. Mechanistically, acetylation of microtubules promotes the release of microtubule-associated RhoGEF, GEF-H1 into the cytoplasm, which then leads to RhoA activation and high actomyosin contractility. Thus, we propose a novel feedback loop involving a crosstalk between microtubules and actin in mechanotransduction at focal adhesions whereby, cells sense the rigidity of the substrate through integrin-mediated adhesions, modulate their levels of microtubule acetylation, which then controls the actomyosin cytoskeleton and force transmission on the substrate to promote mechanosensitive cell migration.

2021-11-02 | PXD015871 | Pride

Nuclear Talin-1 Provides a Bridge Between Cell Adhesion and Gene Expression

Project description:Nuclear Talin-1 Provides a Bridge Between Cell Adhesion and Gene Expression

| PRJNA814198 | ENA

G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [Ribo-Seq]

Project description:The subcellular localization of mRNAs plays a pivotal role in biological processes, including cell migration. For instance, β-actin mRNA and its associated RNA binding protein (RBP), ZBP1/IGF2BP1, are recruited to focal adhesions (FAs), to support localized β-actin synthesis, crucial for cell migration. However, whether other mRNAs and RBPs also localize at FAs remains unclear. Here, we identify hundreds of mRNAs that are enriched at FAs (FA-mRNAs). FA-mRNAs share characteristics with stress granule (SG) mRNAs and are found in ribonucleoprotein (RNP) complexes with the SG RBP. Mechanistically, G3BP1 binds to FA proteins in an RNA-dependent manner, and its RNA-binding and dimerization domains, essential for G3BP1 to form RNPs in SG, are required for FA localization and cell migration. We find that G3BP1 RNPs promote cell speed by enhancing FA protein mobility and FA size. These findings suggest a previously unappreciated role for G3BP1 RNPs in regulating FA function under non-stress conditions.

2024-04-20 | GSE246955 | GEO

G3BP1 Ribonucleoprotein Complexes Regulate Focal Adhesion Protein Mobility and Cell Migration [RNA-seq]

2024-04-20 | GSE246499 | GEO

Remodeling of the focal adhesion complex by hydrogen-peroxide- induced senescence

Project description:Cellular senescence is a phenotype characterized by cessation of cell division, which can be caused by exhaustive replication or environmental stress. It is involved in age-related pathophysiological conditions and affects both the cellular cytoskeleton and the prime cellular mechanosensors, focal adhesion complexes. While the size of focal adhesions increases during senescence, it is unknown if and how this is accompanied by a remodeling of the internal focal adhesion structure. Our study uses metal-induced energy transfer to study the axial dimension of focal adhesion proteins from oxidative-stress-induced senescent cells with nanometer precision, and compares these to unstressed cells. We influenced cytoskeletal tension and the functioning of mechanosensitive ion channels using drugs and studied the combined effect of senescence and drug intervention on the focal adhesion structure. We find that H 2 O 2 induced restructuring of the focal adhesion complex indicates a loss of tension and altered talin complexation. Mass spectroscopy-based proteomics confirmed the differential regulation of several cytoskeletal proteins induced by H 2 O 2 treatment.

2023-07-06 | PXD041766 | Pride

Sub-compartment specific small non-coding RNA expression deregulation and altered nucleoli in mesial temporal lobe epilepsy

Project description:Large scale changes in coding and non-coding RNA expression is a common feature of the resected hippocampal tissue from pharmacoresistant mesial temporal lobe epilepsy (mTLE) patients. However, there is very less insight on the expression and localization changes of the key regulatory RNAs at a sub-compartment level contributing to pathological mechanisms in mTLE. In the present study we set out to understand the global sub-compartment specific changes in miRNA expression and localization and the alterations in the nucleus that possibly drive these changes and the consequences towards mTLE pathogenesis. We compared the nuclear and cytoplasmic distribution of miRNAs by small RNA-seq in subcellular fractionations of hippocampal tissue from mTLE patients and controls. Several miRNAs were found to be specifically enriched in the nucleus of hippocampal cells from patients compared to the controls, where miR-92b-3p (a miRNA-enriched in neurons) was the most de-regulated nuclear miRNA. By performing miR-92b co-immunoprecipitation (co-IP) assay on N2A nuclei and RNA-seq we identified enrichment of mTLE relevant pathways involving mitochondrial and ribosomal processes.

2024-11-05 | GSE269625 | GEO

Expression data from different levels of ANA in HIV+ people

Project description:Different focal adhesions, gap junction, adherens junction, and tight junction, TLR signaling pathway were seen when compared the HIV+ high ANA (anti-nuclear antibodies) group with low ANA group We used microarrays to detail the global programme of gene expression underlying cellularisation and identified distinct classes of up-regulated genes during this process.

2018-10-01 | GSE101589 | GEO

U2OS Adhesion Isolations +/- CytochalasinD and Neomycin

Project description:U2OS cells preferentially utilise integrin alphaV beta5 in adhesion complexes when grown under standard cell culture conditions for 3 days. AlphaV beta5 can be found in both classical 'Focal' adhesions and in novel 'Reticular' adhesions that do not associate with F-actin or other known adhesion protein components. In order to identify components of reticular adhesions, cells were treated with cytochalasinD in order to disrupt F-actin and promote loss of focal adhesions. Remaining reticular adhesion complexes were stabilised with DTBP crosslinking reagent before adhesion complexes were isolated. Preliminary data suggested that depletion of PIP2 by Neomycin treatment would lead to disruption of reticular adhesions preferentially over focal adhesions and so this manipulation was included in these experiments.

2019-06-03 | PXD008680 | Pride

Profiling subcellular localization of nuclear-encoded mitochondrial gene products in zebrafish

Project description:Profiling subcellular localization of nuclear-encoded mitochondrial gene products in zebrafish

| PRJNA705081 | ENA

HNRNPU regulates lncRNAs nuclear localization

Project description:To elucidate the role of HNRNPU in regulation of lncRNAs nuclear localization, we knocked down HNRNPU in K562 cells using short interfering RNAs and performed subcellular RNA-seq using nuclear or cytosolic RNAs

2021-01-23 | GSE165310 | GEO

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