Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomics mass spectrometry after immunoprecipitation of histidine phosphatase in uveal melanoma cells

ABSTRACT: Immunoprecipitation (IP) of histidine phosphatase LHPP proteins for mass spectrometry. Stable LHPP-overexpressing UM Mum2b cells were used to obtain protein lysate. LHPP was used as bait protein for IP. Enriched proteins were colleted and analyzed as the poteintial interacting protein of LHPP.

ORGANISM(S): Homo Sapiens

SUBMITTER: Jian Huang

PROVIDER: PXD050264 | iProX | Fri Mar 01 00:00:00 GMT 2024

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

CRISPR-mediated BMP9 ablation promotes liver steatosis via the down-regulation of PPARα expression.

Yang Z Z Li P P Shang Q Q Wang Y Y He J J Ge S S Jia R R Fan X X

Science advances 20201127 48

Obesity drives the development of nonalcoholic fatty liver disease (NAFLD) characterized by hepatic steatosis. Several bone morphogenetic proteins (BMPs) except BMP9 were reported related to metabolic syndrome. This study demonstrates that liver cytokine BMP9 is decreased in the liver and serum of NAFLD model mice and patients. BMP9 knockdown induces lipid accumulation in Hepa 1-6 cells. BMP9-knockout mice exhibit hepatosteatosis due to down-regulated peroxisome proliferator-activated receptor α ...[more]

PMID: 33246954

Similar Datasets

The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm

Project description:Most members of the phylum Firmicutes harbor a two-component system, LiaSR, which is involved in the response to cell envelope stress elicited most notably by inhibitors of the lipid II cycle. In all LiaSR systems studied in detail LiaSR-mediated signal transduction was shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR homolog of Listeria monocytogenes (LiaSRLm). Whole genome transcriptional profiling indicated that activation of LiaSRLm results in a remodeling of the cell envelope via the massive upregulation of membrane or cell-wall associated proteins in the presence of inducing stimuli. As shown for other LiaSR two-component systems LiaSRLm is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaRLm, which is required for the induction of the LiaSRLm regulon, is controlled by the interplay between histidine kinase and phosphatase activity of the bifunctional sensor protein LiaSLm. Our data suggest that the phosphatase activity of LiaSLm is stimulated by LiaF in the absence of cell envelope stress A total of three independently isolated RNA samples from each strain were used for the analysis.

2010-11-16 | E-GEOD-24107 | biostudies-arrayexpress

Histidine to glutamine substitutants, a regulated process that impacts cell survival and suggests histidine shortage in cancer

Project description:Cancer-associated genetic, epigenetic, and microenvironmental factors impose shortages of tryptophan and arginine, which induce specific codon reassignments (substitutants) in their proteomes. Whether cancers are deprived of other amino acids is unknown. Histidine is an essential amino acid reported to be low in certain tumor types. Therefore, we investigated the potential for a histidine shortage in cancer. Using cultured cancer cells, we pinpointed histidine to glutamine (H>Q) substitutants as the most pronounced proteomic event following histidine deprivation. We then scanned cancer proteomes for H>Q proteins and observed a marked enrichment in pancreatic, uterine, and kidney cancers. Mechanistically, we propose that H>Q is a result of tRNA misalignment, and used tRNA glutamine (tRNA(Gln)) modifications at the wobble position to demonstrate it. We further show that URM1-mediated U34 thiolation boosts H>Q production and influences the survival of cancer cells following histidine deprivation, suggesting a potential role for H>Q. Additional characterization of H>Q substitutants revealed preferred sequences and the maintenance of H>Q host protein expression despite the absence of histidine, indicating cellular regulation and functional consequences. Thus, histidine shortage induces H>Q substitutants, a regulated mistranslation event that pinpoints histidine limitation in cancer and impacts cell survival.

2026-06-29 | GSE330343 | GEO

The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm

2010-11-16 | GSE24107 | GEO

WGS histidine overproducers

Project description:Whole genomes sequencing to determine mutations in histidine overproducers generated with a toxic histidine analog

| PRJEB45772 | ENA

Widespread protein histidine phosphorylation in bacteria

Project description:For decades, extreme difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in E. coli. Our new approach generated the largest E. coli phosphoproteome dataset to date, of which a remarkable high percentage (~10%) are phosphohistidine sites. This resource enables a major step forward towards a better understanding of the biological function of histidine phosphorylation.

2017-12-07 | PXD008369 | JPOST Repository

METTL18-mediated histidine methylation on RPL3 modulates translation elongation for proteostasis maintenance.

Project description:Protein methylation occurs predominantly on lysine and arginine residues, but histidine also serves as a substrate for the modification. However, a limited number of enzymes responsible for this modification have been reported. Moreover, the biological role of histidine methylation has remained poorly understood. Here, we report that human METTL18 is a histidine methyltransferase for the ribosomal protein RPL3 and that the modification specifically slows ribosome traverse on tyrosine codons, allowing the proper folding of synthesized proteins. By performing an in vitro methylation assay with a methyl donor analog and quantitative mass spectrometry, we found that His245 of RPL3 is methylated at the τ-N position by METTL18. Structural comparison of the modified and unmodified ribosomes showed stoichiometric modification and suggested a role in translation tuning. Indeed, genome-wide ribosome profiling revealed suppressed ribosomal translocation at tyrosine codons by RPL3 methylation. Because the slower elongation provides enough time for nascent protein folding, RPL3 methylation protects cells from the cellular aggregation of Tyr-rich proteins. Our results reveal histidine methylation as an example of a “ribosome code” that ensures proteome integrity in cells.

2022-06-15 | GSE200172 | GEO

METTL18-mediated histidine methylation on RPL3 modulates translation elongation for proteostasis maintenance

Project description:In addition to predominant protein methylation on lysine and arginine residues, histidine also serves as a substrate for the modification. However, a limited number of enzymes responsible for this modification has been reported. Moreover, the biological mission of the histidine methylation has remained poorly understood. Here, we reported that human METTL18 is a histidine methyltransferase for ribosomal protein RPL3 and that the modification specifically slows ribosome traverse on tyrosine codons, allowing proper folding of synthesized proteins. Harnessing in vitro methylation assay with methyl-donor analogue and quantitative mass spectrometry, we identified that His245 of RPL3 is methylated at τ-N position by METTL18. Structural comparison of the modified and unmodified ribosomes showed the stoichiometric modification and suggested its role in translation tuning. Indeed, genome-wide ribosome profiling revealed the suppressed ribosomal translocation at tyrosine codons by RPL3 methylation. Because the slower elongation provides enough time for nascent protein folding, RPL3 methylation protects cells from cellular aggregation of Tyr-rich proteins. Our results reveal histidine methylation as an example of “ribosome code”, which ensures proteome integrity in cells.

2022-06-15 | GSE179854 | GEO

Toxoplasma protein phosphatase PPKL Co-IP MS data

Project description:Toxoplasma protein phosphatase PPKL Co-IP MS data of the paper "The protein phosphatase PPKL is a key regulator of daughter parasite development in Toxoplasma gondii".

| MSV000092841 | MassIVE

Histidine-dependent protein methylation is required for compartmentalization of CTP synthase

Project description:CTP synthase (CTPS) forms compartmentalized filaments in response to substrate availability and environmental nutrient status. However, the physiological role of filaments and mechanisms for filament assembly are not well understood. Here, we provide evidence that CTPS forms filaments in response to histidine influx during glutamine starvation. CTPS protein levels remained stable in the presence of histidine during nutrient deprivation, followed by rapid cell growth following nutrient replenishment. Tetramer conformation-based filament formation restricted CTPS enzyme activity duringnutrient deprivation. Furthermore, we demonstrated that filament formation controlled at two levels. Starvation stress/glutamine deficiency activates the GCN2/ATF4/MTHFD2 axis to accelerate the folate cycle in mitochondria for energy homeostasis. In addition, histidine promotes re-methylation of homocysteine by donating one-carbon to the cytosolic folate cycle. CTPS filament formation induced by histidine-mediated methylation maybe a strategy usedby cancer cells to maintain homeostasis and ensure a growth advantage in adverse environments.

2018-08-29 | GSE105251 | GEO

HUVEC Gene Regulation by Histidine-Rich Glycoprotein

Project description:HRG is a 75kDa heparin-binding protein non to extert gene regultaion changes on macropahges. To assess the effect of HRG on Enodothelial Cell gene regulation Human Umbilical Vein Endothelial Cells (HUVECs) were treated with Histidine-Rich Glycoprotein (HRG) 24 hour treatment with HRG. and examined for gene regulation changes versus untreated HUVECs after 6 and

2015-03-12 | GSE66768 | 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