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Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [3A]

ABSTRACT: Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [3A]

PROVIDER: PRJNA1105634 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28824456.fastq.gz	Fastqsanger.gz
	SRR28824457.fastq.gz	Fastqsanger.gz
	SRR28824458.fastq.gz	Fastqsanger.gz
	SRR28824459.fastq.gz	Fastqsanger.gz
	SRR28824460.fastq.gz	Fastqsanger.gz

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Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [3A]

Project description:Metabolic disorder is emerging as a crucial contributor to the pathogenesis of diabetic vascular complications including diabetic retinopathy (DR), the leading cause of blindness in the working-age population. Yet, the underlying molecular mechanisms of how the disturbed metabolic homeostasis contribute to vascular dysfunction in DR remain elusive. O-GlcNAcylation modification act as a nutrient sensor particularly sensitive to ambient glucose. Here, we observed pronounced O-GlcNAc elevation in retina endothelial cells (ECs) of DR patients and mouse models. Endothelial-specific depletion or pharmacological inhibition of O-GlcNAc transferase efficiently mitigated vascular dysfunctions. Mechanistically, we found that YAP/TAZ, key effectors of the Hippo pathway, are O-GlcNAcylated in DR. We identified Thr383 as an O-GlcNAc site on YAP, which inhibits its phosphorylation at Ser397, leading to its stabilization and activation. Consequently, highly activated YAP/TAZ, promotes vascular dysfunction by inducing a pro-angiogenic and glucose metabolic transcriptional program. These findings emphasize the critical role of O-GlcNAc-Hippo axis in DR pathogenesis and suggest its unique potential as a therapeutic target.

2024-09-24 | GSE266071 | GEO

Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [9A]

Project description:Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [9A]

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Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy [9A]

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Immunoprecipitation of YAP - Protein O-GlcNAcylation coupled to Hippo signaling drives vascular dysfunction in diabetic retinopathy

Project description:YAP was immunoprecipitated to detect O-GlcNAcylation status.

2024-10-27 | PXD056603 | Pride

GlcNAcylation of histone H2B facilitates its monoubiquitination

Project description:This SuperSeries is composed of the following subset Series: GSE33049: GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data] GSE33050: GlcNAcylation of histone H2B facilitates its monoubiquitination [Affymetrix data] Refer to individual Series

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GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

Project description:We report that histone GlcNAcylation of H2B S112 is a vital histone modification which facilitates histone monoubiquitination (ub). In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over entire chromosomes including transcribed gene loci, together with co-localization of H2B S112 GlcNAcylation and K120 ub. Examination of H2B S112 GlcNAc and H2B K120 ub in HeLa S3 cells

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GlcNAcylation of histone H2B facilitates its monoubiquitination [Illumina Genome Analyzer data]

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Project description:The development of diabetic retinopathy is well characterized on a histological level. Early vascular alterations involve the loss of pericytes. Earlier mechanisms leading to the phenotype of diabetic retinopathy, which involves the complete neurovascular unit, are not yet fully understood. The gene expression data presented here is derived from microarrays and gives further insights into early genetic regulation in incipient diabetic retinopathy.

2019-01-17 | GSE111465 | GEO

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