Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions

ABSTRACT: A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions

PROVIDER: PRJNA336438 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions [ChIP-seq]

Project description:We have identified that expression of constitutive active Smad3 (Smad3CA) significantly enhanced reprogramming by Oct4, Sox2, Klf4, c-Myc. Smad3 is known to interact with several master transcription factors and boost their activity during development. Therefore, we hypothesized that Smad3CA is recruited to Oct4 binding sites during reprogramming. To test this hypothesis, we investigated genome-wide Smad3 binding sites in the presence and absence of reprogramming factor expression.

2017-11-03 | GSE85177 | GEO

A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions [ATAC-seq]

Project description:We have identified that expression of constitutive active Smad3 (Smad3CA) significantly enhanced reprogramming by Oct4, Sox2, Klf4, c-Myc. To investigate how Smad3CA expression impacts on chromatin opening, we performed ATAC-seq on day 3 of reprogramming in the presence or absence of Smad3CA expression.

2017-11-03 | GSE85175 | GEO

Mus musculus

Project description:A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions [ATAC-seq]

| PRJNA336447 | ENA

Mus musculus

Project description:A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions [ChIP-seq]

| PRJNA336441 | ENA

A general transcription co-factor, Smad3, potentiates master transcription factor mediated cell identity conversions

Project description:This SuperSeries is composed of the SubSeries listed below.

2017-11-02 | GSE85178 | GEO

SMAD3 targets in A549 lung epithelial cells

Project description:TGFβ activates a signal transduction cascade that results in the transcription of genes, primarily through the DNA-binding transcription factor SMAD3. The objective of this study is to identify SMAD3 binding targets and the molecular pathways affected by the TGFβ1/SMAD3 signal transduction on a genome-wide scale.

2011-06-24 | GSE26858 | GEO

SMAD3 targets in A549 lung epithelial cells

Project description:TGF? activates a signal transduction cascade that results in the transcription of genes, primarily through the DNA-binding transcription factor SMAD3. The objective of this study is to identify SMAD3 binding targets and the molecular pathways affected by the TGF?1/SMAD3 signal transduction on a genome-wide scale. Cultured A549 cells at 30-50% confluence were treated with 10 uM SIS3 in dimethyl sulfoxide (DMSO), or DMSO (vehicle-only) 30 min prior to TGF?1 treatment. Cells were treated with 2 ng/mL recombinant TGF?1 for 0, 2, 12, and 24 h.

2011-06-24 | E-GEOD-26858 | biostudies-arrayexpress

Endothelial OTUD1 promotes Ang II-induced vascular remodeling by deubiquitinating SMAD3

Project description:Understanding the molecular mechanisms of pathological vascular remodeling is important for treating cardiovascular diseases and complications. Recent studies have highlighted a role of deubiquitinases in vascular pathophysiology. In this study, we investigated the role of a deubiquitinase, OTUD1, in angiotensin II (Ang II)-induced vascular remodeling. We identified upregulated OTUD1 in the vascular endothelium of Ang II-challenged mice and showed OTUD1 deletion attenuated vascular remodeling, collagen deposition, and EndMT. Conversely, OTUD1 overexpression aggravated these pathological changes both in vivo and in vitro. Mechanistically, SMAD3 was identified as a substrate of OTUD1 using co-immunoprecipitation followed with LC-MS/MS. We found OTUD1 stabilizes SMAD3 and facilitates SMAD3/SMAD4 complex formation and subsequent nuclear translocation through both K48- and K63-linked deubiquitination. OTUD1-mediated SMAD3 activation regulate the transcription of genes involved in vascular EndMT and remodeling in HUVECs. Finally, SMAD3 inhibition reversed OTUD1-promoted vascular remodeling. Our findings demonstrate endothelial OTUD1 promoted Ang II-induced vascular remodeling by deubiquitinating SMAD3. This study identified SMAD3 as a target of OTUD1 and indicates OTUD1 as a potential therapeutic target for the diseases related to vascular remodeling.

2022-12-24 | PXD037926 | Pride

Identification of Death-promoting transcription factor Btf down stream targets by microarray.

Project description:Death-promoting transcription factor Btf has been reportedly implicated in the apoptotic signal triggered by ionizing radiation, DNA damage-inducing agents, and cyclic stretch. However, mechanisms for the regulation of Btf-mediated apoptosis remain largely unknown. In the present study, we performed genome-wide mRNA expression profiling from Btf-depleted Hela cells and identified SMAD3 as a potential downstream target of Btf. Btf interacted with the SMAD3 promoter and this interaction was associated with the activation of SMAD3 gene transcription. Furthermore, we provided evidence that SMAD3 is involved in the induction of apoptosis, and that the disruption of Btf-mediated SMAD3 expression leads to resistance to DNA damage-induced apoptosis

2016-08-31 | GSE53663 | GEO

Heat shock factor 1 specifically potentiates c-MYC-mediated transcription independently of the canonical heat-shock response

Project description:Despite its pivotal roles in biology, how the transcriptional activity of c-MYC is attuned quantitatively remain poorly defined. Here, we show that heat shock factor 1 (HSF1), the master transcriptional regulator of the heat-shock response, acts as a key modifier of the c-MYC-mediated transcription. HSF1 deficiency diminishes c-MYC DNA binding and dampens its transcriptional activity genome-widely. Mechanistically, c-MYC, MAX, and HSF1 assemble into a transcription factor complex on DNAs and, surprisingly, the DNA binding of HSF1 is dispensable. Instead, HSF1 physically recruits the histone acetyltransferase GCN5, thereby promoting histone acetylation and augmenting c-MYC transcriptional activity. Thus, our studies reveal that HSF1 specifically potentiates the c-MYC-mediated transcription, distinct from its role in the canonical heat-shock response. Importantly, this mechanism of action engenders two distinct c-MYC activation states, primary and advanced, which may be important to accommodate diverse physiological and pathological conditions.

2023-05-22 | GSE199462 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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