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Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE205064 | GEO | 2022/12/15

REPOSITORIES: GEO

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Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [RNA-Seq]

Project description:In this study, we show that histone variant H3.3 is overexpressed in ARMS patient-derived cell lines and patient tumour specimens. Functionally, knockdown of H3F3A significantly impairs the ability of ARMS cells to undertake migration and invasion and reduces Rho activation in vitro. In addition, a striking reduction in metastatic tumour burden and improved survival is apparent in vivo. Through RNA-sequencing and ChIP-sequencing analyses, we identified Melanoma Cell Adhesion Molecule (MCAM/CD146) as a direct downstream target of H3.3. Therefore, this study identifies a novel H3.3- MCAM axis involved in ARMS metastatic phenotypes, and supports the development of MCAM as a therapeutic target for this disease.

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Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [ChIP-Seq]

2022-12-15 | GSE203614 | GEO

Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma

Project description:Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma

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Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [ChIP-Seq]

Project description:Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [ChIP-Seq]

| PRJNA841595 | ENA

Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [RNA-Seq]

Project description:Histone variant H3.3 promotes experimental metastasis in alveolar rhabdomyosarcoma [RNA-Seq]

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Histone H1 binding is restricted by histone variant H3.3

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

2009-10-15 | GSE16885 | GEO

Histone variant H3.3 facilitates open chromatin at promoters.

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

2023-01-25 | GSE186687 | GEO

Histone H1 binding is inhibited by histone variant H3.3.

Project description:Linker histones are involved in the formation of higher-order chromatin structure and the regulation of specific genes, yet it remains unclear what their principal binding determinants are. We generated a genome-wide high-resolution binding map for linker histone H1 in Drosophila cells, using DamID. H1 binds at similar levels across much of the genome, both in classic euchromatin and heterochromatin. Strikingly, there are pronounced dips of low H1 occupancy around transcription start sites for active genes and at many distant cis-regulatory sites. H1 dips are not due to lack of nucleosomes; rather, all regions with low binding of H1 show enrichment of the histone variant H3.3. Knockdown of H3.3 causes H1 levels to increase at these sites, with a concomitant increase in nucleosome repeat length. These changes are independent of transcriptional changes. Our results show that the H3.3 protein counteracts association of H1, providing a mechanism to keep diverse genomic sites in an open chromatin conformation.

| S-EPMC2790488 | biostudies-literature

The histone H3 variant H3.3 regulates gene body DNA methylation

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

2017-04-24 | GSE96873 | GEO

The double face of the histone variant H3.3.

Project description:Histone proteins wrap DNA to form nucleosome particles that compact eukaryotic genomes while still allowing access for cellular processes such as transcription, replication and DNA repair. Histones exist as different variants that have evolved crucial roles in specialized functions in addition to their fundamental role in packaging DNA. H3.3--a conserved histone variant that is structurally very close to the canonical histone H3--has been associated with active transcription. Furthermore, its role in histone replacement at active genes and promoters is highly conserved and has been proposed to participate in the epigenetic transmission of active chromatin states. Unexpectedly, recent data have revealed accumulation of this specific variant at silent loci in pericentric heterochromatin and telomeres, raising questions concerning the actual function of H3.3. In this review, we describe the known properties of H3.3 and the current view concerning its incorporation modes involving particular histone chaperones. Finally, we discuss the functional significance of the use of this H3 variant, in particular during germline formation and early development in different species.

| S-EPMC3193428 | biostudies-other

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