Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Depletion of Erk1 and Erk2 MAP kinases in primary human keratinocytes

ABSTRACT: We assessed the effect of RNAi-mediated MAP kinase cascade signaling blockade in primary human keratinocytes. Two sets of siRNA targeting different regions of the Erk1/2 genes were used, enabling identification of off-target siRNA effects.

ORGANISM(S): Homo sapiens

PROVIDER: GSE15417 | GEO | 2009/05/03

SECONDARY ACCESSION(S): PRJNA115823

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Depletion of Erk1 and Erk2 MAP kinases in primary human keratinocytes

Project description:We assessed the effect of RNAi-mediated MAP kinase cascade signaling blockade in primary human keratinocytes. Two sets of siRNA targeting different regions of the Erk1/2 genes were used, enabling identification of off-target siRNA effects. Primary human keratinocytes were electroporated with scrambled control siRNA, a pair of siRNA oligomers against Erk1 and Erk2 (set A), or an independent pair of siRNA oligomers against Erk1 and Erk2 (set B). Four days after electroporation, RNA was harvested. Three biological replicates were performed for each of the three siRNA groups.

2009-05-03 | E-GEOD-15417 | biostudies-arrayexpress

ERK1 and ERK2 Map Kinases: Specific Roles or Functional Redundancy?

Project description:The MAP kinase signaling cascade Ras/Raf/MEK/ERK has been involved in a large variety of cellular and physiological processes that are crucial for life. Many pathological situations have been associated to this pathway. More than one isoform has been described at each level of the cascade. In this review we devoted our attention to ERK1 and ERK2, which are the effector kinases of the pathway. Whether ERK1 and ERK2 specify functional differences or are in contrast functionally redundant, constitutes an ongoing debate despite the huge amount of studies performed to date. In this review we compiled data on ERK1 vs. ERK2 gene structures, protein sequences, expression levels, structural and molecular mechanisms of activation and substrate recognition. We have also attempted to perform a rigorous analysis of studies regarding the individual roles of ERK1 and ERK2 by the means of morpholinos, siRNA, and shRNA silencing as well as gene disruption or gene replacement in mice. Finally, we comment on a recent study of gene and protein evolution of ERK isoforms as a distinct approach to address the same question. Our review permits the evaluation of the relevance of published studies in the field especially when measurements of global ERK activation are taken into account. Our analysis favors the hypothesis of ERK1 and ERK2 exhibiting functional redundancy and points to the concept of the global ERK quantity, and not isoform specificity, as being the essential determinant to achieve ERK function.

| S-EPMC4897767 | biostudies-literature

RNA-sequencing analysis of mouse liver with a global ERK1, hepatocyte-specific ERK2 or double ERK1/2 knockout

Project description:The analysis examined the effects of a global ERK1 and/or tamoxifen-inducible, hepatocyte-specific ERK2 knockout on the liver transcriptome. Transcriptomes from the livers with a ERK1/2 double knockout were compared to the livers of mice with an ERK1 or ERK2 knockout.

2021-08-13 | GSE181803 | GEO

Changes in gene expression in the striatum of Drd2Cre; ERK1/ERK2 knockout mice

Project description:We knocked out ERK1 and ERK2 in the striatopallidal population of striatal medium spiny neurons and analyzed differences in gene expression at P17, a time of increased synapse formation. We used whole gene microarray to assess transcriptional changes that occur in the mouse striatum at P17 in response to ERK1/2 deletion in striatopallidal medium spiny neurons.

2017-07-25 | GSE93844 | GEO

Transcription profiling of mouse WT Erk1 and Erk2 deficient CD8 T cells

Project description:Comparison of unstimulated and in vitro activated wild type and Erk1 or Erk2 deficient CD8 T cells

2008-10-07 | E-MEXP-1833 | biostudies-arrayexpress

Transcription profiling of ERK1 and ERK2 knockdown in zebrafish embryos at blastula stage

Project description:ERK1 and ERK2 MAPKs are intensively studied signaling proteins that are involved in numerous cellular processes and signaling networks. However, their specific functions in embryonic development remain elusive. The upstream activation pathways for ERK1 and ERK2 are considered to be highly similar, and also many of their downstream targets are considered as common, but still relatively few in vivo downstream targets of these kinases have been identified conclusively. Recent mice studies indicate distinct roles for both ERKs in cellular proliferation, oncogenic transformation and development. <br><br>Microarray experiments were performed to compare morpholino mediated knockdown of ERK1 versus ERK2 in zebrafish development. These two conditions were compared to a standard control morpholino condition. To exclude possible effects of the control morpholino at a transcriptional level, we also performed the transciptome-analysis of the control morpholino, to an injection control (injection with phenol red).

2008-01-01 | E-MEXP-1163 | biostudies-arrayexpress

Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38?.

Project description:Hematopoietic tyrosine phosphatase (HePTP) regulates orthogonal MAP kinase signaling cascades by dephosphorylating both extracellular signal-regulated kinase (ERK) and p38. HePTP recognizes a docking site (D-recruitment site, DRS) on its targets using a conserved N-terminal sequence motif (D-motif). Using solution nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we compare, for the first time, the docking interactions of HePTP with ERK2 and p38?. Our results demonstrate that ERK2-HePTP interactions primarily involve the D-motif, while a contiguous region called the kinase specificity motif also plays a key role in p38?-HePTP interactions. D-Motif-DRS interactions for the two kinases, while similar overall, do show some specific differences.

| S-EPMC3548032 | biostudies-literature

Effect of depletion of AIM2 on gene expression in psoriatic NETs-treated primary human keratinocytes

Project description:To investigate the function of the NET-AIM2 axis on keratinocyte activation during psoriasis, we established psoriatic NETs-treated primary human keratinocytes in which AIM2 has been knocked down by siRNA

2022-10-28 | GSE216519 | GEO

RNA-sequencing analysis of mouse liver with a global ERK1, hepatocyte-specific ERK2 or double ERK1/2 knockout

Project description:RNA-sequencing analysis of mouse liver with a global ERK1, hepatocyte-specific ERK2 or double ERK1/2 knockout

| PRJNA753503 | ENA

P2X7 receptor activates extracellular signal-regulated kinases ERK1 and ERK2 independently of Ca2+ influx.

Project description:P2X7 nucleotide receptors modulate a spectrum of cellular events in various cells including epithelia, such as exocrine pancreas. Although the pharmacology and channel properties of the P2X7 receptors have been studied intensively, signal transduction pathways are relatively unknown. In this study we applied a heterologous expression system of rat P2X7 receptors in HEK-293 cells. We followed the receptor expression and function using the enhanced green fluorescent protein (EGFP) tag, activation of intracellular proteins and increases in cellular Ca2+. EGFP-P2X7 receptors localized to the plasma membrane, clusters within the membrane and intracellularly. Stimulation of P2X7 receptors in HEK-293 cells led to an activation of extracellular signal-regulated kinases ERK1 and ERK2 and this activation was seen after just 1 min of stimulation with ATP. Using C- and N-terminal P2X7-receptor mutants we show that the N-terminus is important in activation of ERKs, whereas deletion of the last 230 amino acids in the C-terminus did not effect ERK activation. On the other hand, Ca2+ entry was impaired in C-terminal but not in N-terminal mutants. In cell suspensions prepared from rat pancreas we show that P2X7 receptors also activate ERK1 and ERK2, indicating that these signalling pathways are also turned on in native epithelium.

| S-EPMC1223572 | biostudies-other

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