Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Gene expression changes in REH following CDC42 inhibition

ABSTRACT: ARHGEF4 expression is associated with t(12;21) acute lymphoblastic leukaemia (ALL). Our study investigated the substrate specificity of ARHGEF4, a member of the diffuse B-cell lymphoma (DBL) family of guanine nucleotide exchange factors (GEFs), in t(12;21) ALL REH cells. ARHGEF4 was found to activate the small guanine nucleotide binding protein (GTPase) CDC42. In order to determine the function of CDC42 in t(12;21) ALL cells, we performed RNAseq analysis on REH cells treated for 24 hours with DMSO vehicle control in comparison to 25uM ML141, a CDC42 inhibitor.

ORGANISM(S): Homo sapiens

PROVIDER: GSE152836 | GEO | 2020/06/20

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Gene expression changes in REH following CDC42 inhibition

Project description:Gene expression changes in REH following CDC42 inhibition

| PRJNA640612 | ENA

Ota2015 - Positive regulation of Rho GTPase activity by RhoGDIs as a result of their direct interaction with GAPs (GDI integrated)

Project description:This is a ordinary differential equation mathematical model describing the Rho GTPase cycle in which Rho GDP-dissociation inhibitors (RhoGDIs) inhibit the regulatory activities of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) by interacting with them directly as well as by sequestering the Rho GTPases. The model was constructed with the intent of analyzing the role of RhoGDIs in Rho GTPase signaling.

2019-12-17 | BIOMD0000000899 | BioModels

Gene expression changes in REH following STAT3 inhibition by shRNA

Project description:STAT3 (Signal transducer and activator of transcription 3) expression is associated with with t(12;21) acute lymphoblastic leukaemia (ALL) and it is crucial for the survival of the t(12;21) ALL . Our study investigated the STAT3 regulated pathways and discovered a novel STAT3-TP53 axis in B-ALL. In order to determine the STAT3 regulated pathways in t(12;21) ALL cells, we performed RNAseq analysis on the Pre-B Acute Lymphoblastic Leukemia (ALL) cell line REH following shRNA-mediated STAT3 knockdown

2024-01-31 | GSE179332 | GEO

Gene expression changes in REH following STAT3 pharmacological inhibition

2024-01-31 | GSE179333 | GEO

Homo sapiens

Project description:Extracellular Superoxide Dismutase Regulates the Expression of GTPase Guanine Nucleotide Exchange Factors (GEFs), GTPase-activating proteins (GAPs), and Rho Guanine nucleotide disassociation inhibitors (GDI)

| PRJNA243869 | ENA

Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism

Project description:Rho GTPases regulate actin dynamics and cell motility, and their hyperactivation drives cancer metastasis1. P-Rex (PI(3,4,5)P3-dependent Rac Exchanger) guanine nucleotide exchange factors (GEFs) are potent on-switches for Rho GTPase signalling and are frequently dysregulated in metastatic cancer2. P-Rex GEFs are autoinhibited under basal conditions and activated synergistically by binding to Gβγ and PI(3,4,5)P33. However, the molecular basis for P-Rex autoinhibition remains unknown. Here we utilise X-ray crystallography, cryo-EM and cross-linking mass spectrometry to determine the autoinhibited P-Rex1 structure. P-Rex1 forms a characteristic bipartite structure with its seven domains split into distinct N- and C-terminal modules. The two modules are connected by a previously unrecognised C-terminal four-helix bundle that binds the N-terminal Pleckstrin homology (PH) domain. In the N-terminal module, the catalytic surface of the Dbl homology (DH) domain is occluded by the compact arrangement of the PH and DEP1 domains. Structural analysis of the DH-PH-DEP1 array reveals that a remarkable conformational transition, centred on a 126° opening of a hinge helix reminiscent of calmodulin dynamics, leads to the release of DH domain autoinhibition. Furthermore, given the off-axis position of the Gβγ and PI(3,4,5)P3 binding sites, our data suggest that concurrent Gβγ and PI(3,4,5)P3 requires counter-rotation of the two halves of P-Rex1 by 90°, leading to the uncoupling of the PH domain from the four-helic¬¬al bundle, and release of the autoinhibited DH domain to drive Rho GTPase signalling.

2022-08-12 | PXD034327 | Pride

Gene expression profiles of Treg cells lacking Cdc42 GTPase

Project description:Gene expression profiles of Treg cells lacking Cdc42 GTPase

| PRJNA753464 | ENA

Homo sapiens isolate:REH

Project description:REH MultiOmics

| PRJNA600820 | ENA

Expression data of liver tissue from wild type and Cdc42 liver-specific knockout mice at 2-month-old

Project description:Hepatocellular carcinoma (HCC) is one of the leading causes of cancer-related death. However, the mechanism for HCC initiation remains poorly known. Cdc42, a small Rho GTPase, with multiple cellular functions has been shown involved in variant types of human cancers, but its role in HCC initiation remains unclear. Cdc42 liver-specific knockout mice (Cdc42LK) developed HCC at 6-month-old. We used microarrays to detail the global programme of gene expression induced by Cdc42 deletion and identified distinct classes of up or down-regulated genes during HCC initial time.

2021-01-01 | GSE147433 | GEO

Cdc42 controls DC-maturation - Cdc42-dependent actin dynamics controls maturation and secretory activity of dendritic cells

Project description:Cell division cycle 42 (Cdc42) is a member of the Rho GTPase family and has pivotal functions in actin organization, cell migration and proliferation. Cdc42 has been shown to regulate antigen (Ag)-uptake in immature dendritic cells (DC) and controls their migration from tissues to lymph nodes. Previous reports demonstrated that Cdc42 is inactivated upon DC-maturation to avoid continued Ag-acquisition. To further study the molecular mechanisms of DC-control by Cdc42, we used bone marrow-derived DCs from Cdc42-deficient mice. We show that Cdc42-deficient DCs are phenotypically mature without additional maturation stimuli, as they upregulate CD86 from intracellular storages to the cell surface. They also accumulate invariant chain (Ii)-MHC class II complexes at the cell surface, which cannot efficiently present peptide Ag for priming of Ag-specific CD4 T cells. Lack of Cdc42 in immature DCs does not allow MHC class II maturation, as lysosomal Cathepsins are lost into the supernatant and Ii-MHC class II complexes cannot mature. Therefore Cdc42-deficient DCs are "pseudomature" and lose most functional hallmarks of antigen-presenting cells. Our results propose that Cdc42 keeps DCs in an immature state, while downregulation of Cdc42-activity during maturation facilitates generation of CD86+MHCII+ mature DCs.

2015-10-12 | PXD001934 | Pride

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