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Rhes, a striatal enriched protein, regulates SUMOylation of nuclear proteins and gene expression in a SUMO-dependent manner

ABSTRACT: Rhes, a striatal enriched protein, regulates SUMOylation of nuclear proteins and gene expression in a SUMO-dependent manner

PROVIDER: PRJNA634335 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11825850_1.fastq.gz	Fastqsanger.gz
	SRR11825850_2.fastq.gz	Fastqsanger.gz
	SRR11825851_1.fastq.gz	Fastqsanger.gz
	SRR11825851_2.fastq.gz	Fastqsanger.gz
	SRR11825852_1.fastq.gz	Fastqsanger.gz

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Rhes, a striatal enriched protein, regulates SUMOylation of nuclear proteins and gene expression in a SUMO-dependent manner

Project description:Rhes, a multifunctional striatal protein, regulates nuclear proteins and gene expression via SUMO-mediated mechnisms.

2020-11-23 | GSE150990 | GEO

Rhes, a striatal enriched protein regulates post-translational Small-Ubiquitin like-Modifier (SUMO) Modification of nuclear proteins and alters gene expression

Project description:Rhes (Ras homolog enriched in the striatum) is a multifunctional protein that orchestrates striatal toxicity, motor behaviors and abnormal movements associated with dopaminergic signaling, Huntington disease and Parkinson disease signaling in the striatum. Rhes engineers membranous tunneling nanotube-like structures and promotes intercellular proteinand cargoes transport. Recent study revealed Rhes also regulates mitophagy via the Nix receptor. Despite these studies, the mechanisms through which Rhes mediates these diversefunctions remains unclear. Rhes belongs to a small GTPase family member and consists of a unique C-terminal Small Ubiquitin-like Modifier (SUMO) E3-like domain that promotes the post-translational modification (PTM) of proteins with SUMO (SUMOylation) by promoting “cross-SUMOylation” of SUMO enzymes SUMO E1 (Aos1/Uba2) and SUMO E2 ligase (Ubc-9). However, the identity of the SUMO substrates of Rhes remains largely unknown. By combining high throughput 47 interactome and SUMO proteomics we report that Rhes regulates the SUMOylation of nuclear proteins that are involved in the regulation of gene transcription. While Rhes has increased the SUMOylation of histone deacetylase 1 (HDAC1) and histone 2B, it had decreased the SUMOylation of heterogeneous nuclear ribonucleoprotein M (HNRNPM), protein polybromo-1(PBRM1) and E3 SUMO-protein ligase (PIASy). We also found that Rhes itself is SUMOylated at 5 different lysine residues (K32, K110, K114, K120, K124 and K245). Furthermore, we found that Rhes regulates the expression of genes involved in cellular morphogenesis and differentiation in the striatum, in a SUMO-dependent manner. Our findings thus provide a previously undescribed role for Rhes in regulating SUMOylation of nuclear targets and in orchestrating striatal gene expression via the SUMOylation.

2024-06-10 | PXD023394 | Pride

Uncovering Global SUMOylation Signaling Networks in a Site-Specific Manner

Project description:SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreover, for the first time in excess of 1,000 SUMOylation sites were identified under standard growth conditions. SUMOylation dynamics were quantitatively studied in response to SUMO protease inhibition, proteasome inhibition and heat shock.

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SUMO and RNAPolII chromatin profiling in SUMOylation-competent and -deficient bone marrow derived dendritic cells unstimulated or stimulated with LPS

Project description:Purpose: To determine SUMO1 and SUMO2 chromatin profile in a static and dynamic manner in BMDC before and after LPS stimulation, and to determine RNAPolII chromatin occupancy in sumoylation-deficient BMDC compared to wild-type cells. Methods: SUMO1, SUMO2 and RNAPolII chromatin profiles were determined by sequencing BMDC chromatin immunoprecipitated with antibodies specific for SUMO1, SUMO2 and RNAPolII before and after LPS stimulation. Results: We show dynamic occupancy of three distal sites upstream of Ifnb1 gene by SUMO1 and SUMO2, as well as increased RNAPolII recruitment on selected genes. Conclusions: SUMO acts as a regulator of inflammatory and anti-viral gene programs. A study of SUMO and RNAPolII chromatin profile in Bone Marrow derived Dendritic Cells.

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Gene expression profiles in wild-type and SUMO knockdown mice after forebrain ischemia

Project description:Transient brain ischemia massively activates global SUMOylation. A large fraction of SUMO targets are nuclear proteins involved in gene expression. However, gene expression profile modulated by ischemia-induced SUMOylation has not been studied. Using a SUMO knockdown (SUMO-KD) mouse model and microarray technique, we investigated how SUMOylation modulated gene expression after brain ischemia. Wild-type and SUMO-KD mice were subjected to transient forebrain ischemia or sham surgery. The hippocampal CA1 subfield samples collected at 3 hours reperfusion were analyzed using Affymetrix microarrays.

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Gene expression profiles in wild-type and SUMO knockdown mice after forebrain ischemia

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2021-12-31 | GSE163682 | GEO

Auto-sumoylation of the Ubc9 E2 SUMO-conjugating Enzyme Extends Cellular Lifespan (RNA-Seq)

2024-04-17 | GSE254981 | GEO