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Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [GRO-Seq]

ABSTRACT: Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [GRO-Seq]

PROVIDER: PRJNA590194 | ENA |

REPOSITORIES: ENA

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Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses

Project description:Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses

| PRJNA590241 | ENA

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [GRO-Seq]

Project description:Histone deacetylase 3 (HDAC3) is unique among the HDAC superfamily of chromatin modifiers that silence transcription through enzymatic modification of histones, because interaction with nuclear receptor corepressors (NCoR1/2) is required for engagement of its catalytic activity. However, loss of HDAC3 also represses transcription. Here we report that, during lipopolysaccharide (LPS) activation of macrophages, the deacetylase activity of HDAC3 is selectively engaged at ATF3-bound enhancers that repress anti-inflammatory genes. By contrast, LPS-stimulated recruitment of HDAC3 to ATF2-bound sites without NCoR1/2 activates pro-inflammatory genes by a non-canonical mechanism whereby catalytically inactive HDAC3 stably interacts with p65. Consistent with this bimodal inflammatory modulation, deletion of HDAC3 in macrophages safeguards mice from lethal exposure to LPS, but this protection is not conferred by genetic or pharmacological abolition of HDAC3 catalytic activity. Thus, HDAC3 is a dichotomous transcriptional activator and repressor whose deacetylase-independent functions are critical in priming the innate immune system.

2020-04-30 | GSE140573 | GEO

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [ChIP-Seq]

Project description:Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [ChIP-Seq]

| PRJNA590208 | ENA

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [RNA-Seq]

Project description:Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [RNA-Seq]

| PRJNA590243 | ENA

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [RNA-Seq]

2020-04-30 | GSE140610 | GEO

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [ChIP-Seq]

2020-04-30 | GSE140581 | GEO

Dichotomous engagement of HDAC3 activity governs inflammatory responses.

Project description: Not available

| S-EPMC7725280 | biostudies-literature

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses

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

2020-04-30 | GSE140611 | GEO

Circadian Epigenomic Control of Skeletal Muscle Fuel Metabolism by HDAC3

Project description:We address the function of HDAC3 in skeletal muscle metabolism We performed HDAC3 ChIP-seq, RNA-seq, and GRO-seq in mouse muscles at different times of the day and compared between WT and HDAC3-depleted muscles.

2016-09-06 | E-GEOD-79696 | biostudies-arrayexpress

Discovery of a Highly Potent and Selective HDAC3 and HDAC8 PROTAC Dual Degrader

Project description:HDAC3 and HDAC8 are members of class I deacetylases involved in several biological mechanisms and represent a highly sought-after therapeutic target for drug development. It is historically challenging to develop selective deacetylase inhibitors due to their conserved catalytic domains. HDAC3 also has deacetylase-independent activity, which cannot be blocked by conventional enzymatic inhibitors. Recent advances in proteolysis-targeting chimeras (PROTACs) provides an opportunity to eliminate the whole protein selectively, abolishing both enzymatic and scaffolding functions. Here, we report a novel HDAC3/8 dual degrader YX968 that induces highly potent, rapid and selective degradation of both HDAC3 and HDAC8 without trigging pan-HDAC inhibitory effects. Unbiased quantitative proteomics experiments further confirmed its high selectivity. This dual-specific degrader specifically ablates cellular pathways attributed to HDAC3 and HDAC8 and exhibits high potency in killing cancer cells. YX968 represents a new probe for dissecting the complex biological functions of HDAC3 and HDAC8.

2023-07-18 | PXD040941 | Pride

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