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Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

ABSTRACT: Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

PROVIDER: PRJNA956455 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24187721.fastq.gz	Fastqsanger.gz
	SRR24187721_1.fastq.gz	Fastqsanger.gz
	SRR24187721_2.fastq.gz	Fastqsanger.gz
	SRR24187722.fastq.gz	Fastqsanger.gz
	SRR24187722_1.fastq.gz	Fastqsanger.gz

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Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

Project description:Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

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Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

Project description:Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

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Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

Project description:The global loss of heterochromatin during aging has been observed in eukaryotes from yeast to humans, and this has been proposed to be one of the causes of aging. However, the cause of this age-associated loss of heterochromatin has remained enigmatic. Here we show that heterochromatin markers, including histone H3K9 di-/tri-methylation and HP1, decrease with age in murine muscle stem cells (MuSCs) as a consequence of the depletion of the methyl donor SAM. We find that restoration of intracellular SAM in aged MuSCs restores heterochromatin content to youthful levels and rejuvenates age-associated features including DNA damage accumulation, increased cell death, and defective muscle regeneration. SAM is not only a methyl group donor for transmethylation but it is also an aminopropyl donor for polyamine synthesis. Excessive consumption of SAM in polyamine synthesis may reduce its availability for transmethylation. Consistent with this premise, we observe that perturbation of increased polyamine synthesis by inhibiting spermidine synthase (Srm) restores the intracellular SAM content as well as heterochromatin formation, leading to improvements in aged MuSC function and regenerative capacity. Together, our studies demonstrate a direct causal link between polyamine metabolism and epigenetic dysregulation during MuSC aging.

2023-11-17 | GSE229851 | GEO

Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

2023-11-17 | GSE229853 | GEO

Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing.

Project description: Not available

| S-EPMC10976122 | biostudies-literature

Depletion of SAM leading to loss of heterochromatin drives muscle stem cell ageing

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

2023-11-17 | GSE229854 | GEO

Modelling mitochondrial SAM depletion in fruit flies and mice

Project description:S-adenosylmethionine (SAM) is the principle biological methyl group donor for a diverse range of substrates. It is synthesised in the cytosolic methionine cycle and shuttled throughout the cell. The mitochondrial SAM (mitoSAM) pool depends on import through the inner-membrane SAMC and supports the maturation of metabolites and mitochondrial RNAs. Mutations in SAMC in patients cause a severe metabolic crisis, however, the organellar regulation of mitoSAM and the protein methylation landscape within mitochondria are largely unknown. Using fly and mouse models, we demonstrate that titrating mitoSAM differentially effects mitochondrial function. Metabolite and iron-sulfur cluster biosynthesis are disrupted due to acutely decreased methylation potential, while prolonged mitoSAM deficiency affects fly longevity and OXPHOS stability. The herein uploaded raw data was used for total larvae and total cell proteome quantification in the established lines. Our results define the critical role of cytoplasmic SAM production for mitochondrial methylation events and highlight the indirect effect of one-carbon metabolism on cellular bioenergetics.

2021-02-22 | PXD019550 | Pride

Depletion of Sun1/2 Induces Heterochromatin Accrual in MSCs

Project description:Depletion of Sun1/2 Induces Heterochromatin Accrual in MSCs

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Keap1 governs ageing-induced protein aggregation in endothelial cells

Project description:The breach of proteostasis, leading to the accumulation of protein aggregates, is a hallmark of ageing and age-associated disorders, up to now well-established in neurodegeneration. Few studies have addressed the issue of dysfunctional cell response to protein deposition also for the cardiovascular system. However, the molecular basis of proteostasis decline in vascular cells, as well as its relation to ageing, are not understood. Recent studies have indicated the associations of Nrf2 transcription factor, the critical modulator of cellular stress-response, with ageing and premature senescence. In this report, we outline the significance of protein aggregation in physiological and premature ageing of murine and human endothelial cells (ECs). Our study shows that aged donor-derived and prematurely senescent Nrf2-deficient primary human ECs, but not those overexpressing dominant-negative Nrf2, exhibit increased accumulation of protein aggregates. Such phenotype is also found in the aortas of aged mice and young Nrf2 tKO mice. Ageing-related loss of proteostasis in ECs depends on Keap1, well-known repressor of Nrf2, recently perceived as a key independent regulator of EC function. Ageing-induced deposition of protein aggregates in ECs is associated with impaired autophagy and can be counteracted by Keap1 depletion or rapamycin treatment. Our results show that Keap1:Nrf2 protein balance predominates Nrf2 transcription-dependent mechanisms in governing proteostasis and ageing in ECs.

2020-08-12 | PXD018969 | Pride

The U6 snRNA m6A methyltransferase METTL16 regulates SAM synthetase intron retention

Project description:Maintenance of the intracellular levels of the methyl donor S-adenosylmethionine (SAM) is essential for a wide variety of biological processes. We demonstrate that the N6-adenosine methyltransferase METTL16 regulates expression of MAT2A, which encodes the only SAM synthetase expressed in most cells. Upon SAM depletion by methionine starvation, cells induce MAT2A expression by enhanced splicing of a retained intron. Induction requires METTL16 and its methylation substrate, a vertebrate conserved hairpin (hp1) in the MAT2A 3´ UTR. Increasing METTL16 occupancy on the MAT2A 3´ UTR is sufficient to induce efficient splicing. We propose that under SAM-limiting conditions, METTL16 occupancy on hp1 increases due to inefficient enzymatic turnover, which in turn promotes MAT2A splicing. Interestingly, human and S. pombe METTL16 methylate the U6 spliceosomal snRNA at a sequence identical to hp1. These observations suggest that the conserved U6 snRNA methyltransferase evolved an additional function in vertebrates to regulate SAM homeostasis.

2017-05-18 | GSE90914 | GEO

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