Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Association of heme bound HRI with S-DELE1 promotes structural re-arrangements within the HRI kinase domain

ABSTRACT: This dataset assesses structural changes occurring in human, heme-bound HRI upon association with S-DELE1. To this end, human HRI and S-DELE1 were expressed EIF2alpha phosphorylation-resistent cells supplemented with hemin. HRI was affinity purified, crosslinked with DSS, and structural changes in HRI were assessed by MS. The data set identifies S-DELE1 induced structural changes in the C-terminal region and the kinase insert of HRI, as well as domains of HRI that are in structural proximity to S-DELE1.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Barbara Steigenberger

LAB HEAD: Lucas Jae

PROVIDER: PXD063587 | Pride | 2026-05-07

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	202401217_EXPL6_Neo_BaSt_SA_Orbi5445_sample01.raw	Raw
	202401217_EXPL6_Neo_BaSt_SA_Orbi5445_sample01_Crosslinks.txt	Txt
	202401217_EXPL6_Neo_BaSt_SA_Orbi5445_sample02.raw	Raw
	202401217_EXPL6_Neo_BaSt_SA_Orbi5445_sample02_Crosslinks.txt	Txt
	202401217_EXPL6_Neo_BaSt_SA_Orbi5445_sample03.raw	Raw

Items per page:

1 - 5 of 16

Similar Datasets

Association of heme-bound HRI with S-DELE1 promotes HRI auto-phosphorylation

Project description:This dataset assesses the effects of S-DELE1 association on the auto-phosphorylation of human, heme-bound HRI. Human HRI and DELE1 were expressed in EIF2alpha-phospho-resistant cells supplemented with hemin. HRI was affinity purified, the elution subjected to denaturing gel electrophoresis, and HRI phosphorylation was assessed by MS. The data set identifies S-DELE1 induced phosphorylation sites in the N-terminal domain of HRI, its two kinase domains, and the kinase insert.

2026-06-09 | PXD062916 | Pride

Human HRI Autophosphorylation Profile

Project description:Heme-regulated inhibitorRegulated Inhibitor (HRI) is one of the four mammalian kinases that phosphorylate eIF2α, facilitating a cellular response to stress through the regulation of mRNA translation. Originally identified as a heme sensor in erythroid progenitor cells, HRI has since emerged as a potential therapeutic target in both cancer and neurodegeneration. Here we purified recombinant expressed human HRI and allowed it to autophosphorylate.

2025-06-18 | PXD064940 | Pride

Composite SMG5-1 SMG6 PIN domain formation is essential for NMD

Project description:Nonsense-mediated mRNA decay (NMD) relies on the coordinated assembly and action of multiple protein factors. Degradation of target mRNAs begins with endonucleolytic cleavage near premature stop codons, but the mechanisms of endonuclease activation and regulation remain unclear. Using structural predictions, biochemical in vitro assays, and cell-based NMD analysis, we show that SMG5 and SMG6 interact via their PIN domains to form a composite interface (cPIN) with full endonuclease activity. In vitro reconstituted SMG5-SMG6 cPIN heterodimers show high activity, as SMG5 completes the SMG6 active site and substrate binding site. Mutations in residues at their predicted interaction surfaces, RNA-binding sites, or active-site attenuate or abolish cPIN activity in vitro and impair cellular NMD. Our findings demonstrate how paralogous PIN domains complement each other to assemble a highly active endonuclease in NMD, providing a structural and mechanistic explanation for efficient NMD substrate degradation.

2026-01-30 | PXD072588 | Pride

Determination of protein monoclonal-antibody epitopes by a combination of structural proteomics methods.

Project description:We use a combination of multiple structural proteomics techniques (differential photo-reactive surface modification, HDX, crosslinking and epitope excision/extraction) for the determination of the protein antigen epitopes for monoclonal antibodies.

2023-10-24 | PXD040902 | Pride

OMA1, DELE1 and HRI relay mitochondrial stress to the mammalian integrated stress response

Project description:The goal of this study is to understand how mamalian cells respond to the mitochondial stress. Using Quant-seq, we identifed an integrated stress response signature in the cells with compromized mitochondria. Furthermore, using an unbiased CRISPRi genetic screen, we uncovered a novel signaling pathway, in which OMA1, DELE1 and HRI are three major players that relay the mitochondrial stress to the integated stress response. To further study the cellular response in the absence of this pathway, we again used Quant-seq to uncover alternative pathways that might play a role during the mitochondrial stress response.

2019-07-29 | GSE134986 | GEO

OMA1, DELE1 and HRI relay mitochondrial stress to the mammalian integrated stress response

Project description:OMA1, DELE1 and HRI relay mitochondrial stress to the mammalian integrated stress response

| PRJNA557038 | ENA

Thriving in the heat – Lysine acetylation stabilizes the quaternary structure of a Mega-Dalton hyperthermoactive PEP-synthase

Project description:Over time structural adaptations enabled proteins and enzymes to have sufficient stability and flexibility to perform the basic functions of life under various environmental conditions. The catalytic cores of key metabolic enzymes of hyperthermophilic archaea work at a temperature range of 80-120 °C, similar to the conditions wher the earliest life forms may have thrived. Here we characterize a key enzyme of the central carbon metabolism of Pyrococcus furious, through an integrative approach combining structural mass spectrometry, cryo-electron microscopy, mass photometry and molecular modelling with molecular dynamics simulations. From our investigation, we unveil the structural organization of phosphoenolpyruvate synthase (PPSA). Its 24-meric assembly - weighing over 2 MDa - harbors flexible distal domains, whose proper functioning and coordination depends on widespread chemical acetylation of lysine residues. This non-enzymatic post-translational modification, along with other types of lysine modifications, also occurs on most other major protein complexes of P. furiosus. These modifications likely originated in the chemically favorable primordial conditions and gradually became highly specialized and enzyme-driven in more distantly related mesophiles and Eukaryotes.

2022-08-08 | PXD035847 | Pride

Evolutionarily conserved spliceosome-exosome pathway in nuclear mRNA surveillance

Project description:Intron-containing mRNAs are co-transcriptionally spliced and assembled into messenger ribonucleoprotein (mRNP) particles, a process monitored by surveillance pathways. Here, we combined biochemical and structural approaches to elucidate the mechanisms by which mRNPs are sorted between two opposing fates: nuclear degradation or cytoplasmic export. The human LENG8-PCID2 complex operates as an mRNP-decay connector, coupling nuclear mRNPs to the RNA-degrading exosome via the PAXT adaptor complex, while the related GANP-PCID2 complex connects mRNPs to the nuclear pore complex. Both recognize the mRNP component UAP56, but LENG8-PCID2 uniquely associates with early splicing factors through a direct interaction with U1A and RRP1B. Notably, the Thp3-Csn12 ortholog in budding yeast also serves as an mRNP-decay connector, coupling the early splicing factors Mud2-Bbp with the nuclear exosome. The spliceosome-exosome mRNP-decay pathway we uncovered reveals molecular principles that remain strikingly conserved across evolution, despite the fundamental differences in splicing and decay between humans and budding yeast.

2026-05-18 | PXD071678 | Pride

Abundance analysis of chromatin-residing proteins during lineage conversion using protein aggregation capture (PAC)

Project description:We performed abundance analysis of chromatin-residing proteins in BLaER1 cells during the early stages of B-cell-to-macrophage transdifferentiation. We employed protein aggregation capture (PAC) to analyze chromatin-residing protein abundances at 0, 6 and 24 h after induction of transdifferentiation in the absence and presence of the small-molecule SUMOylation inhibitor ML-792 (SUMOi). Mass spectrometry analyses were executed with high resolution mass spectrometry (LC-MS), using the Evosep One liquid chromatography system coupled to Orbitrap Astral mass spectrometer. Raw Orbitrap Astral data-independent acquisition (DIA) data were processed with DIA-NN. Data ouput from DIA-NN were further processed with ProteoGyver.

2026-05-27 | PXD076495 | Pride

Determination of autophosphorylation sites of human HRI

Project description:This dataset assesses the effects of DELE1 on Succinylacetone (SA)- and dihydroartemisinin (DHA)-induced auto-phosphorylation of endogenous human HRI, as well as the heme-dependent repression of HRI auto-phosphorylation. This dataset identifies DELE1-induced phosphorylation sites in the second kinase domain and the kinase insert and phosphorylation sites in the second kinase domain and the kinase insert that are repressed by hemin.

| PXD074030 | panorama

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