Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Ribosomal protein S6 phospho-deficient mice display altered novelty-induced locomotion, synaptic plasticity, and specific mRNA translation

ABSTRACT: By high-throughput RNA-seq of heavy polysomal fractions, we report that rpS6 knockin mice, in which the 5 phosphorylatable serines have been replaced by alanines, show an alteration in the translation, but not transcription, of a subset of mRNAs in the nucleus accumbens (NAc) but not in the dorsal striatum (DStr). Gene Ontology analysis revealed that multiple dysregulated mRNAs are related to the mitochondria. Moreover, we described that rpS6 knockin mice also display an alteration in novelty-induced locomotion and synaptic plasticity.

ORGANISM(S): Mus musculus

PROVIDER: GSE98029 | GEO | 2018/02/23

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

Phosphorylation of Ribosomal Protein S6 differentially affects mRNA translation based on ORF length

Project description:Phosphorylation of Ribosomal Protein S6 (RPS6) was the first post-translational modification of the ribosome to be identified and is a commonly-used readout for mTORC1 activity. Although the cellular and organismal functions of RPS6 phosphorylation are known, its molecular consequences on translation are less well understood. Here we use selective ribosome footprinting to analyze the location of ribosomes containing phosphorylated RPS6 on endogenous mRNAs in cells. We find that RPS6 becomes progressively dephosphorylated on ribosomes as they translate an mRNA. As a consequence, average RPS6 phosphorylation is higher on mRNAs with short coding sequences (CDSs) compared to mRNAs with long CDSs. Loss of RPS6 phosphorylation causes a correspondingly larger drop in translation efficiency of mRNAs with short CDSs than long CDSs. Interestingly, mRNAs with 5’ TOP motifs are translated well also in the absence of RPS6 phosphorylation despite short CDS lengths, suggesting they are translated via a different mode. In sum this provides a dynamic view of RPS6 phosphorylation on ribosomes as they translate mRNAs and the functional consequence on translation.

2021-12-22 | GSE168977 | GEO

Ribosomal protein S6 Rps6 heterozygous null deletion effect on footpad epidermis

Project description:Mutant and non-mutant footpad. McGowan et al. in press Keywords: Mutant vs. non-mutant The tissue (footpad epidermis) is from a conditional heterozygous null deletion of Rps6. One copy of Rps6 was deleted from keratinocytes in the skin using the K5.Cre transgene. K5Cre x Rps6^loxP

2008-06-12 | E-GEOD-11331 | biostudies-arrayexpress

Effect of conditional deletion of S6 ribosomal protein following partial hepatectomy

Project description:Deletion of the RPS6 gene in mouse liver results in the inhibition of 40S ribosome biogenesis and the failure of hepatocytes to enter S-phase following partial hepatectomy. This microarray experiment was designed to assess the effects of RPS6 deletion on the expression of genes involved in liver regeneration following partial hepatectomy. Keywords: time course, liver RNA was isolated from mouse livers at different time-points following partial hepatectomy. Conditional deletion of the RPS6 gene was perfomed by injecting polyinosinic-polycytidylic acid in mice harbouring a floxed version of the RPS6 gene and a cre recombinase under the regulation of an interferon responsive promoter (MX-CRE). The mice used a control have also a floxed version of the RPS6 gene but lack the cre recombinaste transgene.

2009-05-01 | E-GEOD-13864 | biostudies-arrayexpress

Ribosomal Protein S6 Phosphorylation Is Involved in Novelty-Induced Locomotion, Synaptic Plasticity and mRNA Translation.

Project description: Not available

| S-EPMC5742586 | biostudies-literature

Ribosomal protein S6 Rps6 heterozygous null deletion effect on footpad epidermis

2008-06-12 | GSE11331 | GEO

mRNA expression data from livers of wild-type (WT) mice, mice that lack ribosomal protein S6 (Rps6) (DS6), mice that overexpress c-Myc (Myc) and livers that lack Rps6 and also overexpress c-Myc (DS6 Myc)

Project description:Targeted depletion of ribosomal protein S6 (Rps6) from hepatoblasts of the developing liver results in neonatal sub-lethal hepatic failure due to inhibition of bile duct development and widespread induction of hepatocyte death triggering regeneration. Overexpression of c-Myc is hepatoprotective in the context of Rps6-deficiency and eliminates the need for DS6 livers to regenerate by preventing hepatocyte death. Microarrays were used to identify the transcriptional program associated with loss of hepatic Rps6 and to identify mRNAs associated with c-Myc's hepatoprotective effect in DS6 livers

2023-01-04 | GSE212363 | GEO

Effect of conditional deletion of S6 ribosomal protein following partial hepatectomy

2009-05-01 | GSE13864 | GEO

Translatome analysis of Mycobacterium tuberculosis

Project description:We present the data obtained from high-resolution ribosome profiling analysis of Mycobacterium tuberculosis grown under standard conditions (log phase) and cells subjected to oxidative stress (50 µM cumene hydroperoxide) and pH stress (pH 4.5). Our data shows pervasive ribosome pausing in the M. tb translatome. A large number of genes show very high pause immediately downstream to the translation start site. Moreover, serines and alanines in the E site of the ribosome exhibit highest pause scores.

2021-06-02 | GSE151718 | GEO

Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation (limited proteolysis experiment)

Project description:The charged linker region in Hsp90 has been shown to be important for Hsp90 function and global conformation. In humans, two serines located in the charged linker region are constitutively phosphorylated in vivo. In order to gain knowledge on the possible effect of these phosphorylation sites on Hsp90 global conformation, we purified a human Hsp90β mutant where both serines are mutated to alanines, and used limited proteolysis to study the “proteolytic” fingerprint of our mutant and the wild-type, phosphorylated Hsp90β. We observed that serine to alanine mutation resulted in increased tryptic cleavage in the C-domain of Hsp90β.

2021-07-07 | PXD025878 | Pride

Phospho-site mutants of the RNA Polymerase II C-terminal domain alter subtelomeric gene expression and chromatin modification state in fission yeast

Project description:Eukaryotic gene expression requires that RNA Polymerase II (RNAP II) gain access to DNA in the context of chromatin. The C-terminal domain (CTD) of RNAP II recruits chromatin modifying enzymes to promoters, allowing for transcription initiation or repression. Specific CTD phosphorylation marks facilitate recruitment of chromatin modifiers, transcriptional regulators, and RNA processing factors during the transcription cycle. However, the readable code for recruiting such factors is still not fully defined and how CTD modifications affect related families of genes or regional gene expression is not well understood. Here we examine the effects of manipulating the Y1S2P3T4S5P6S7 heptapeptide repeat of the CTD of RNAP II in Schizosaccharomyces pombe by substituting non-phosphorylatable alanines for Ser2 and/or Ser7 and the phosphomimetic glutamic acid for Ser7. Global gene expression analyses were conducted using splicing-sensitive microarrays and validated via RT-qPCR. The CTD mutations did not affect pre-mRNA splicing or snRNA levels. Rather, the data revealed upregulation of subtelomeric genes and alteration of the repressive histone H3 lysine 9 methylation (HeK9me) landscape. The data further indicate that H3K9me and expression status are not fully correlated, suggestive of CTD-dependent subtelomeric repression mechansims that act independently of H3K9me levels. Splicing sensitive S. pombe microarrays (Agilent-027365) were used to compare the splicing and expression profile of four mutant strains relative to WT control with 3-5 biological replicates and dye flipped samples

2016-08-10 | E-GEOD-83426 | biostudies-arrayexpress

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