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Regulation of the oxidative stress response by the E3 ligase TRIP12

ABSTRACT: Regulation of the oxidative stress response by the E3 ligase TRIP12

PROVIDER: PRJNA1182683 | ENA |

REPOSITORIES: ENA

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Regulation of the oxidative stress response by the E3 ligase TRIP12

Project description:Centered on the transcription factor NRF2, the oxidative stress response counteracts reactive oxygen species (ROS) to ensure cell and tissue homeostasis. While unstressed cells constantly degrade NRF2, ROS inhibit the respective E3 ligase, CUL3KEAP1, to stabilize NRF2 and elicit antioxidant gene expression. Following ROS clearance, cells must rapidly reinstate NRF2 degradation, but mechanisms underlying this dynamic regulation are poorly understood. Here, we identify TRIP12, an essential E3 ligase dysregulated in Clark-Baraitser Syndrome and Parkinson’s Disease, as a component of the oxidative stress response. TRIP12 is a ubiquitin chain elongation factor that acts after CUL3KEAP1 to extend K29-linked conjugates for efficient NRF2 degradation. TRIP12 accelerates stress response silencing as CUL3KEAP1 is being restored, but limits NRF2 activation during stress. The need for dynamic NRF2 regulation therefore comes at the cost of less responsive stress signaling, suggesting that TRIP12 inhibition could be exploited to bolster the oxidative stress response in neurodegenerative diseases.

2025-08-12 | GSE281184 | GEO

The intrinsically disordered region of the E3 ubiquitin ligase TRIP12 induces the formation of chromatin condensates and interferes with DNA damage response.

Project description:Chromatin compaction is crucial for the expression and the integrity of the genome. We previously showed that the nuclear HECT-type E3 ubiquitin ligase TRIP12 (Thyroid hormone Receptor Interacting Protein 12) is tightly associated to chromatin. Overexpressed in several types of cancers, we explored herein the consequences of TRIP12 overexpression on chromatin homeostasis. First, we established the proxisome of TRIP12 by BioID and unveiled its pleiotropic role in chromatin regulation. Second, we demonstrated that an overexpression of TRIP12, via its intrinsically disordered region, leads to the formation of chromatin condensates enriched in heterochromatin epigenetic marks. We further discovered that the formation of TRIP12 mediated-chromatin condensates is highly dynamic and driven by a mechanism of polymer-polymer phase separation (PPPS). Chromatin condensates formation is dependent not only on the concentration, the length of TRIP12-IDR but also electrostatic interactions. Chromatin compaction is a determinant parameter in several biological processes. Indeed, we measured that the formation of TRIP12 mediated-chromatin condensates alters cell cycle progression, genome accessibility, transcription as well as DNA damage response (DDR) by inhibiting the accumulation of Mediator DNA Damage Checkpoint (MDC1). Altogether, this study reveals a novel dynamic role for TRIP12 in chromatin compaction independently of its ubiquitin ligase activity with important consequences on cellular processes.

2026-02-11 | GSE242544 | GEO

Trip12 deficiency effect on embryonic stem cell line

Project description:Analysis of E14 embryonic stem cells lacking Trip12 ubiquitin ligase activity. We used microarrays to detail the global gene expression profiles affected by Trip12 ubiquitin ligase activity in mouse embryonic stem cell. Total RNA was extracted from wild-type and Trip12 mutant mouse embryonic stem cells and hybridized on Affymetrix microarrays.

2014-01-01 | E-GEOD-27527 | biostudies-arrayexpress

E3 ubiquitin ligase TRIP12 catalyzes non-canonical lysine-independent ubiquitin-ubiquitin linkages in vitro

Project description:Mass spectrometry raw data and proteomic results relating to: E3 ubiquitin ligase TRIP12 catalyzes non-canonical lysine-independent ubiquitin-ubiquitin linkages in vitro

2025-05-23 | MSV000097978 | MassIVE

Transcriptomic profiling of human pancreatic cancer-derived cell lines MiaPACA-2 depleted of TRIP12 mRNA compared to control cells

Project description:TRIP12 (Thyroid hormone Receptor Interacting Protein) is an E3 ubiquitin ligase involved in numerous cellular processes. TRIP12 controls the stability of the PTF1A transcription factor that is implicated in pancreatic cancer initiation. To elucidate the role of TRIP12 on the expression of pancreatic cancer-derived cell lines, Trip12 mRNA expression was inhibited using a shRNA strategy. Transcriptomic profiling of shTrip12-MiaPACA-2 cell s was perfomed and compared to ShScramble control cells.

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Transcriptomic profiling of human pancreatic cancer-derived cell lines PANC-1 depleted of TRIP12 mRNA compared to control cells

Project description:TRIP12 (Thyroid hormone Receptor Interacting Protein) is an E3 ubiquitin ligase involved in numerous cellular processes. TRIP12 controls the stability of the PTF1A transcription factor that is implicated in pancreatic cancer initiation. To elucidate the role of TRIP12 on the expression of pancreatic cancer-derived cell lines, Trip12 mRNA expression was inhibited using a shRNA strategy. Transcriptomic profiling of shTrip12-PANC-1 cell s was perfomed and compared to ShScramble control cells.

2024-04-19 | GSE147717 | GEO

Trip12 deficiency effect on embryonic stem cell line

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Effect of depletion of TRIP12 on gene expression in adult murine pancreatic acinar cells and murine pancreatic cancer cell lines

Project description:To investigate the role of the E3 ubiquitin ligase Thyroid Receptor Interacting Protein 12 (TRIP12) in pancreatic acinar cell identity and pancreatic carcinogenesis, we used genetically engineered mouse models of pancreas-selective Trip12 deletion, mutant Kras (G12D) and mutant P53 (R172H). We performed gene expression analysis using RNA-seq data from adult acinar cells. We established cell lines from murine pancreatic tumors.

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E3 ubiquitin ligase TRIP12 controls protein translation and promotes cancer cell survival via a potential mTOR/G3BP1 nexus

Project description:Mass spectrometry data and proteomic results relating to the manuscript: E3 ubiquitin ligase TRIP12 controls protein translation and promotes cancer cell survival via a potential mTOR/G3BP1 nexus

2025-06-19 | MSV000098264 | MassIVE

E3 ligase TRIP12 affecting EZH2 ubiquitination in ENKTL

Project description:Effects of potential E3 ligase that mediates polyubiquitination of EZH2 in extranodal natural killer T cell lymphoma

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