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TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 1)

ABSTRACT: TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 1)

PROVIDER: PRJNA700648 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13657658.fastq.gz	Fastqsanger.gz
	SRR13657659.fastq.gz	Fastqsanger.gz
	SRR13657660.fastq.gz	Fastqsanger.gz

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TRIM28-dependent SUMOylation protects the adult ovary from the male pathway

Project description:TRIM28-dependent SUMOylation protects the adult ovary from the male pathway

| PRJNA700643 | ENA

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 2)

Project description:We study the role of the protein Trim28 in the maintenance of sexual identity of the adult ovary. With the help of conditional knock out (cKO) of Trim28 using the Nr5a1:Cre, we observed that deletion of the Trim28 gene in granulosa cells of the adult ovary induces their transdifferentiation into Sertoli cells, the supporting cell lineage of the testicular seminiferous tubules. FOXL2 expression has disappeared and follicles were completely remodeled into tubular structures with cells that expressed the Sertoli cell markers SOX8, SOX9 and DMRT1. Histological analysis confirmed the progressive reorganization of ovarian follicles into tubular structures and the and the transdifferentiation of granulosa cells by cells with a Sertoli cell morphology. TRIM28 acts as a SUMO-E3 ligase by interacting with the SUMO-E2 conjugating enzyme UBC9 (encoded by the Ube2i gene) via the Plant homeodomain (PHD), and can self-SUMOylate. To study in vivo the role of TRIM28-dependent SUMOylation, we generated a point mutation in exon 13 of mouse Trim28 within the PHD domain of the TRIM28 protein (C651F) that abrogates its SUMO-E3 ligase activity. We generated Trim28Phd/cKO mice (termed PHD mutant). Like in cKO ovaries, FOXL2 expression was undetectable, whereas we observed expression of the Sertoli cell markers SOX9, SOX8 and DMRT1 within structures organized in pseudo-tubules in PHD ovaries. Our results indicate that maintenance of the female pathway in the adult ovary depends on the E3-SUMO ligase activity of TRIM28.

2022-05-24 | GSE166384 | GEO

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (RNA-Seq)

Project description:TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (RNA-Seq)

| PRJNA700646 | ENA

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (RNA-Seq)

2022-05-24 | GSE166382 | GEO

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 2)

Project description:TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 2)

| PRJNA700645 | ENA

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 1)

2022-05-24 | GSE166383 | GEO

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway

Project description:This SuperSeries is composed of the SubSeries listed below.

2022-05-24 | GSE166385 | GEO

TRIM28-dependent SUMOylation protects the adult ovary from activation of the testicular pathway.

Project description: Not available

| S-EPMC9338040 | biostudies-literature

Transcriptome analysis of A549 cells expressing a SUMOylation-deficient TRIM28 mutant in the context of influenza A virus infection

Project description:Aim: Identify differentially expressed genes in human lung epithelial cells expressing a SUMOylation-deficient TRIM28 mutant (TRIM28 6KR) compared to TRIM28 wt.

2019-08-05 | GSE133329 | GEO

TRIM28-Mediated SUMOylation of G3BP1/2 Regulates Stress Granule Dynamics

Project description:Stress granules (SGs) are stress-induced membraneless organelles whose dynamics are tightly regulated by protein interactions and modifications. However, whether SUMOylation directly targets SG core proteins G3BP1/2 and which ligase is involved remains unclear. Capturing these key events while preserving SG integrity is challenging due to their transient and membraneless nature. To address this, we introduce a low-concentration formaldehyde crosslinking (lcFAX) method that stabilizes membraneless organelles, including G3BP1 SGs and TDP-43 nuclear bodies, enabling enhanced proteome identification. Importantly, we identify TRIM28 as a previously undefined SG-associated protein and reveal that TRIM28 SUMOylates G3BP1 at K287 and G3BP2 at K281, establishing a critical mechanism regulating SG dynamics that ultimately impacts cellular ROS and apoptosis. lcFAX-Seq also provides insights into the RNA composition of SGs. Altogether, lcFAX-MS uncovers the critical role of TRIM28-mediated SUMOylation in modulating SG dynamics, establishing lcFAX as a powerful tool for analyzing membraneless organelles and the underlying regulatory mechanisms.

2025-09-24 | GSE286197 | GEO

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