Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

PABPC1 stress granule interactome identified by BioID

ABSTRACT: Identification of Stress Granule interacting proteins by BioID (Roux et al., 2012) using PABPC1-BirA(R118G)-GFP construct

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Triana Amen

LAB HEAD: Daniel Kaganovich

PROVIDER: PXD025334 | Pride | 2022-02-17

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Stress granules inhibit fatty acid oxidation by modulating mitochondrial permeability.

Amen Triana T Kaganovich Daniel D

Cell reports 20210601 11

The formation of stress granules (SGs) is an essential aspect of the cellular response to many kinds of stress, but its adaptive role is far from clear. SG dysfunction is implicated in aging-onset neurodegenerative diseases, prompting interest in their physiological function. Here, we report that during starvation stress, SGs interact with mitochondria and regulate metabolic remodeling. We show that SG formation leads to a downregulation of fatty acid β-oxidation (FAO) through the modulation of ...[more]

PMID: 34133922

Similar Datasets

Fasnall induces atpically transient Stress Granules

Project description:Stress Granule formation has been linked to the resistance of some cancer cells to chemotherapeutic intervention. A number of studies have proposed that certain anti-tumor compounds promote cancer cell survival by inducing Stress Granules formation, leading to increased cellular fitness and apoptosis avoidance. Here we show that a potent fatty acid synthase inhibitor, fasnall, known for its anti-tumor capabilities, triggers the formation of non-canonical Stress Granules with a faster clearing and internal dynamics kinetics independently of fatty acid synthase inhibition. PABPC1 BioID interactomes in fasnall, and arsenite conditions were obtained.

2021-09-09 | PXD021229 | Pride

BioID2(Gly40Ser)-SEC22A proximity biotinylation in HeLa cells

Project description:Proximity labelling using transient expression of the same exogenous BioID2(Gly40Ser)-SEC22A construct in wild-type HeLa cells and in otherwise isogenic RAB3GAP1-, RAB3GAP2- and RAB18-null HeLa cell lines.

2024-01-26 | PXD016404 | Pride

Multi-organ systems study reveals Igfbp7 as a suppressor of gluconeogenesis after gastric bypass surgery

Project description:Roux-en-Y gastric bypass (RYGB) surgery reduces weight in obese patients. A marked decrease in blood glucose levels occurs before weight loss; however, key molecules that improve glycemic profile remain largely unknown. We used the RYGB surgery model in diet-induced obese (DIO) mice to monitor the proteome (with tandem mass tagging) of the Roux and biliopancreatic limbs, the liver and the pancreas up to four weeks after surgery, a time window associated with the early beneficial metabolic effects of the RYGB surgery model. The resulting kinetics were analyzed using high-dimensional cluster analysis that we recently developed (XINA,PMID: 30370770) to infer co-regulated proteins and pathways based on common kinetic profiles. Our analysis revealed the organs exhibited unique and common changes to their proteomes reflecting their specialized physiological roles and potential coordinated inter-organ crosstalk and responses, respectively. Further exploration of the Roux limb proteome kinetics included the identification of relatively unknown proteins found with clusters comprising established protein-protein interaction networks. One such protein was insulin-like growth factor binding protein 7 (Igfbp7) whose subsequent in vitro and in vivo studies supported the role of this secreted protein in suppressing hepatic gluconeogenesis; which in turn, substantiates our systems approach to discover new mechanisms by which the RYGB surgery exerts beneficial effects.

2020-01-23 | PXD015276 | Pride

Proximity-biotinylation (BioID) to dissect cytoplasmic p53 signaling networks under nutrient stress

Project description:p53 signaling is a major response mechanism to cellular stresses through cytoplasmic or nuclear action. While p53 protein levels have been shown to increase upon nutrient stresses such as starvation, the exact signaling cascade in this context remains elusive. Here, we use proximity biotinylation (BioID), to derive the cytoplasmic p53 interaction network as immediate early starvation response.

2022-06-09 | PXD027734 | Pride

Remodeling of Ago2-mRNA interactions upon cellular stress reflects miRNA complementarity and correlates with altered translation rates (part 4)

Project description:When adapting to environmental stress, cells attenuate and reprogram their translational output. In part, these altered translation profiles are established through changes in the interactions between RNA-binding proteins and mRNAs. The Ago2/microRNA machinery has been shown to participate in stress-induced translational upregulation of a particular mRNA, CAT-1; however, a detailed, transcriptome-wide understanding of the involvement of Ago2 in the process has been lacking. Here, we profiled the overall changes in Ago2-mRNA interactions upon arsenite stress by CLIP-seq. Ago2 displayed a significant remodeling of its transcript occupancy, with the majority of 3` UTR and CDS sites exhibiting stronger interaction. Interestingly, target sites that were destined for release from Ago2 upon stress were depleted in miRNA complementarity signatures, suggesting an alternative mode of interaction. To compare the changes in Ago2 binding patterns across transcripts with changes in their translational states, we measured mRNA profiles on ribosome/polysome gradients by RNA-seq. Increased Ago2 occupancy correlated with stronger repression of translation for those mRNAs, as evidenced by a shift toward lighter gradient fractions upon stress, while release of Ago2 was associated with the limited number of transcripts that remained translated. Taken together, these data point to a role for Ago2 and the mammalian microRNAs in mediating the translational component of the stress response. In this sub-series, RNAseq data from sucrose gradient fractions with arsenite treatment are presented.

2013-07-15 | E-GEOD-44379 | biostudies-arrayexpress

Proteome of arsenite in P. pseudoalcaligenes CECT 5344

Project description:Quantitative proteomic analysis of P. pseudoalcaligenes CECT 5344 in the presence of arsenite (As(III)) with ammonium and cyanide as nitrogen sources

2023-05-10 | PXD033539 | Pride

Short poly(A) tails are protected from deadenylation by the LARP1-PABP complex

Project description:To find PABPC1-interactants in cells, PABPC1 immunoprecipitates were analyzed by LC-MS/MS

2022-08-20 | PXD028326 | Pride

BirA*-RAB18 proximity biotinylation in HeLa cells

Project description:Proximity labelling using transient expression of the same exogenous BirA*-RAB18 construct in wild-type HeLa cells and in otherwise isogenic RAB3GAP1-, RAB3GAP2- and TRAPPC9-null HeLa cell lines.

2024-01-26 | PXD016336 | Pride

Paracrine stimulation effect of autologous salispheres and human salispheres on mouse salivary gland

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2015-09-10 | E-GEOD-72871 | biostudies-arrayexpress

Proximity biotinylation and LC-MSMS identification of the molecular microenvironment of coronavirus replication complexes

Project description:To investigate virus-host interactions at the site of coronavirus replication, we developed a biotin-based proximity labelling approach by engineering a promiscuous biotin ligase, BirA-R118G, within the coronavirus replication and transcription complex (RTC). BirA-R118G was fused to non-structural protein 2 to generate MHV- BirA-R118G-nsp2. During the course of infection, viral and host factors in proximity of the viral RTC become covalently biotinylated, allowing affinity purification of biotin-tagged factors and mass spectrometry identification of RTC-proximal viral and host factors. Results provide a comprehensive library of RTC-associated factors which likely include crucial factors that promote, orchestrate and assist viral replication within the viral RTC microenvironment.

2019-01-16 | PXD009975 | 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