Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ABSTRACT: Overexpression of GPR31 with interaction site mutation

PROVIDER: PRJNA1213778 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR32063521.fastq.gz	Fastqsanger.gz
	SRR32063522.fastq.gz	Fastqsanger.gz
	SRR32063523.fastq.gz	Fastqsanger.gz
	SRR32063523_1.fastq.gz	Fastqsanger.gz
	SRR32063523_2.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 20

Similar Datasets

Project description:Overexpression of GPR31 with glycosylation site mutation

| PRJNA1213749 | ENA

Project description:Overexpression of GPR31 in mouse

| PRJNA1213873 | ENA

Project description:Overexpression of GPR31 in primary hepatocytes

| PRJNA1213869 | ENA

Gene expression profiles of each subset of human intestinal mononuclear phagocytes (MNPs)

Project description:MNPs play an important role in intestinal homeostasis. The interaction of intestinal metabolites with G protein-coupled receptors (GPCRs) expressed on human MNPs has not been well characterized. We report here that GPR31 is specifically expressed in cDC1 in human ileal MNPs by bulk RNA sequencing.

2024-10-08 | GSE272657 | GEO

Effect of GPR31-signaling on gene expression in LysoDCs during Listeria monocytogenes infection.

Project description:GPR31 signaling induced dendrite protrusion of lysozyme-expressing dendritic cells (LysoDCs) into basolateral pockets of M cells. To investigate the effect of GPR31 signaling on LysoDC function during infection, we analyzed the gene expression profile of LysoDCs from WT and Gpr31b-deficient mice at 2 days after L. monocytogenes infection.

2025-08-01 | GSE295342 | GEO

Effect of pyruvate (PA), lactate (LA), or 12-hydroxyeicosatetraenoic acid (12-HETE) stimulation on type1 conventional dendritic cells (cDC1) from the human ileum

Project description:We here report that GPR31 is specifically expressed in cDC1 in human intestinal mononuclear phagocytes. Since GPR31 has been previously reported to be activated by PA, LA, and 12-HETE, RNA-seq was performed to analyze the transcriptional changes in human ileal cDC1 under the stimulation of PA, LA, or 12-HETE.

2024-10-08 | GSE240895 | GEO

The G Protein-Coupled Receptor GPR31 Promotes Proinflammatory Responses in Pancreatic Islets and Macrophages II

Project description:In type 1 diabetes (T1D), the innate and adaptive immune systems attack and eventually destroy the insulin-secreting islet β cells. During this process, β cells activate inflammatory signaling pathways that augment the dysfunction and destruction imposed by cellular autoimmunity. The 12-lipoxygenase (12-LOX) pathway produces the pro-inflammatory eicosanoid 12-HETE, which induces oxidative and endoplasmic reticulum stress and results in diminished insulin secretion and apoptosis. The G protein-coupled receptor 31 (GPR31) has been identified as a putative receptor for 12-HETE. In this study, we generated conventional GPR31 knockout mice. To interrogate the role of GPR31 in β cells, we treated islets from wildtype and Gpr31b-/- mice with proinflammatory cytokines and subjected the islets to RNA sequencing. Differentially expressed genes in Gpr31b-/- islets included those pertaining to receptor signaling, inflammation, oxidative stress, and macrophage migration — effects that are reminiscent of 12-LOX inhibition. Bone-marrow derived macrophages from Gpr31b-/- mice had reduced macrophage migration compared to wildtype macrophages. To mimic islet and macrophage inflammation as seen in T1D, wildtype and Gpr31b-/- mice were treated with the pro-diabetic toxin streptozotocin. Compared to wildtype, Gpr31b-/- mice had improved glucose tolerance and preserved β-cell mass. These results are consistent with previously published data using 12-LOX knockout mice and suggests that GPR31 mediates the proinflammatory responses of 12-HETE in the β cell.

2025-01-06 | GSE285039 | GEO

ChEC-seq2 profiling of Crm1, Nucleoporins (nups), and RNA Pol II from budding yeast grown in SDC

Project description:Nuclear pore proteins (Nups) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation in the Gcn4 transcription factor that blocks its interaction with the nuclear pore complex (NPC). This mutation reduces the interaction of Gcn4 with the highly conserved nuclear export factor Crm1/Xpo1. Crm1 and Nups co-occupy enhancers and Crm1 inhibition blocks interaction of the nuclear pore protein Nup2 with the genome. In vivo, Crm1 interacts stably with the NPC. In vitro, Crm1 binds both Gcn4 and Nup2 directly. Importantly, the interaction between Crm1 and Gcn4 requires neither Ran-GTP nor the nuclear export sequence binding site. Finally, Crm1 and Ran-GTP stimulate DNA binding by Gcn4, suggesting that allosteric coupling between Crm1-Ran-GTP binding and DNA binding facilitates docking of transcription factor-bound enhancers at the NPC.

2025-03-24 | GSE288515 | GEO

ChEC-seq2 profiling of yeast Gcn4 and Crm1-T539C localization after treatment with Leptomycin B.

2025-03-24 | GSE288550 | GEO

ChEC-seq2 profiling of Crm1 and Nup2 during degradation of Nup2 or inhibition/degradation of Crm1, respectively

2025-03-24 | GSE288549 | GEO