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HDAC3 is required for self-renewal and metabolism of Ams [CUT&TAG]

ABSTRACT: HDAC3 is required for the maintenance of AM population and proper metabolism through transcription regulation together with ATF2

ORGANISM(S): Mus musculus

PROVIDER: GSE200017 | GEO | 2025/12/31

REPOSITORIES: GEO

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HDAC3 is required for self-renewal and metabolism of Ams [CUT&TAG]

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HDAC3 is required for self-renewal and metabolism of AMs

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RNA profiling changes of HDAC3 knockout AMs

Project description:HDAC3 is required for the maintenance of AM population and proper metabolism

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HDAC3 is required for self-renewal and metabolism of AMs

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

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Separation of transcriptional repressor and activator functions in HDAC3 [CUT&TAG]

Project description:The histone deacetylase HDAC3 is associated with the NCoR/SMRT co-repressor complex and its canonical function is in transcriptional repression, but it can also activate transcription. Here we show that the repressor and activator functions of HDAC3 can be genetically separated in Drosophila. A lysine substitution in the N-terminus (K26A) disrupts its catalytic activity and activator function, whereas a combination of substitutions (HEBI) abrogating the interaction with SMRTER enhance repressor activity beyond wild-type in the early embryo. We conclude that the critical functions of HDAC3 in embryo development involve catalytic-dependent gene activation and non-enzymatic repression by several mechanisms, including tethering of loci to the nuclear periphery.

2023-06-15 | GSE206248 | GEO

Dichotomous Engagement of HDAC3 Activity Governs Inflammatory Responses [ChIP-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 | GSE140581 | GEO

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

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

2020-04-30 | GSE140573 | GEO

RNA profiling changes of HDAC3 knockout AMs

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Nuclear Receptor Corepressors are Required for the Histone Deacetylase Activity of HDAC3 In Vivo

Project description:Histone deacetylase 3 (HDAC3) is an epigenome-modifying enzyme that is required for normal mouse development and tissue-specific functions. In vitro, HDAC3 protein itself has minimal enzyme activity, but gains its histone deacetylation function from stable association with the conserved deacetylase activation domain (DAD) contained in nuclear receptor corepressors NCOR1 and SMRT. Here we show that HDAC3 enzyme activity is undetectable in mice bearing point mutations in the DAD of both NCOR1 and SMRT (NS-DADm), despite normal levels of HDAC3 protein. Local histone acetylation is increased, and genomic HDAC3 recruitment is reduced though not abrogated. Remarkably, the NS-DADm mice are born and live to adulthood, whereas genetic deletion of HDAC3 is embryonic lethal. These findings demonstrate that nuclear receptor corepressors are required for HDAC3 enzyme activity in vivo, and suggest that a deacetylase-independent function of HDAC3 may be required for life. This SuperSeries is composed of the SubSeries listed below. Refer to individual Series.

2013-01-01 | E-GEOD-42541 | biostudies-arrayexpress

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