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Immunomodulatory effects of glucocorticoid-induced leucine zipper (GILZ) expression in murine bone-marrow derived macrophages.

ABSTRACT: Immunomodulatory effects of glucocorticoid-induced leucine zipper (GILZ) expression in murine bone-marrow derived macrophages.

PROVIDER: PRJNA1068618 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27717653.fastq.gz	Fastqsanger.gz
	SRR27717654.fastq.gz	Fastqsanger.gz
	SRR27717655.fastq.gz	Fastqsanger.gz
	SRR27717656.fastq.gz	Fastqsanger.gz
	SRR27717657.fastq.gz	Fastqsanger.gz

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Immunomodulatory effects of glucocorticoid-induced leucine zipper (GILZ) expression in murine bone-marrow derived macrophages.

Project description:Here, we provide evidence for the immunomodulatory effects of glucocorticoid-induced leucine zipper (GILZ) overexpression in macrophages, demonstrating enhanced antibacterial activity, protection from pyroptosis, and altered mitochondrial function. Additionally, our findings reveal a significant impact on MMP activity, suggesting a role for GILZ in influencing extracellular matrix remodeling and wound healing processes. The study contributes to explorations of GILZ in its significance in pro-resolving macrophage functions.

2024-05-13 | GSE254137 | GEO

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Deep mutational scanning of the interaction of JUN's leucine zipper domain and other human bZIPs in different experimental conditions

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Intricate coupling between the transactivation and basic-leucine zipper domains governs the CK2-dependent phosphorylation of ATF4

Project description:Most transcription factors possess at least one long intrinsically disordered transactivation domain that binds to a variety of co-activators and co-repressors and plays a key role in modulating the transcriptional activity. Despite the crucial importance of these mechanisms, the structural and functional basis of transactivation domain in yet poorly understood. Here, we focused on ATF4/CREB-2, an essential transcription factor for cellular stress adaptation. We found that the N-terminal region of the transactivation domain is involved in transient long-range interactions with the basic-leucine zipper domain. In vitro phosphorylation assays with the protein kinase CK2 show that the presence of the basic-leucine zipper domain is required for optimal phosphorylation of the transactivation domain. This study uncovers the intricate coupling existing between the transactivation and basic-leucine zipper domains of ATF4 and highlights its potential functional relevance.

2023-03-11 | PXD029704 | Pride

Leucine zipper-based sorting system enables generation of multi-functional CAR T cells

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Glucocorticoid Induced Leucine Zipper in Lipopolysaccharide Induced Neuroinflammation.

Project description:Glucocorticoids (GCs) are steroid hormones secreted as the end-product of the neuroendocrine stress cascade. Both absence and elevated GC mediate neurotoxic responses, suggesting that a narrow window ranging from physiological to slightly high GC mediate protective responses. The beneficial effects of GC are attributed to the transactivation of regulatory proteins and inhibition mediated by glucocorticoid receptor (GR) interactions with other co-factors. The glucocorticoid induced leucine zipper (GILZ) is a gene strongly upregulated by GC and mediates many of the anti-inflammatory and anti-proliferative effects of GC. Although GILZ is constitutively expressed in many tissues including the brain, the expression has been shown to occur with varying dynamics suggesting that the local milieu modulates its expression with consequent effects on cellular responses. Here we investigated the expression profile of GILZ in lipopolysaccharide (LPS) mediated neuroinflammation model of Alzheimer's disease (AD). Our data suggest that the GILZ expression is downregulated in neuroinflammation correlating inversely with the pro-inflammatory cytokines and innate immune responses.

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INK4A expression in leukemic cells transformed by the v-Myb oncoprotein depends on the integrity of the v-Myb leucine zipper region

Project description:The AMV v-Myb oncoprotein causes oncogenic transformation of myelomonocytic cells in vivo and in vitro. Its transforming capacity is strictly dependent upon the N-terminal DNA binding domain, the central transactivation region, and on the C-terminal domain containing a putative leucine zipper motif. While deletions in the central part of the leucine zipper region or point mutations of critical leucine residues abolish the leukemogenicity of the protein, a small deletion within the N-terminal part (deltaP mutant) preserves almost full in vitro transforming ability and only weakens the leukemogenic potential in vivo. We analyzed the gene expression profiles of ex vivo cultures transformed with either wild type or deltaP mutant of v-Myb. A few tens of genes were found to be significantly and reproducibly differentially expressed between the two cultures. Among them, the transcript of the CDKN2A gene, which is critically involved in the cell cycle progression regulation, showed higher expression in the deltaP mutant transformed cells. In mammals and also some avian species, there are two different mRNAs - ARF and INK4A – transcribed from the CDKN2A locus. It is known that in chickens the locus had been rearranged in evolution and only one mRNA is transcribed. We found that this mRNA encodes both ARF and INK4A and that the INK4A protein translation starts with a GUG codon downstream of the ARF AUG initiation codon and proceeds in a different reading frame. INK4A protein thus exists in chicken cells as well and its negative regulation by v-Myb is a part of the leukemic transformation mechanism. Comparison of expression profiles of chicken monoblasts transformed either by wild type v-myb or its mutated version designated deltaP. Three biological replicates were analyzed for each group.

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INK4A expression in leukemic cells transformed by the v-Myb oncoprotein depends on the integrity of the v-Myb leucine zipper region

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The Cytoskeletal Stress Response Pathway: a homeostatic system driven by Dual Leucine Zipper Kinase (DLK)

Project description:The Cytoskeletal Stress Response Pathway: a homeostatic system driven by Dual Leucine Zipper Kinase (DLK)

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