Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs

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

ORGANISM(S): Homo sapiens

PROVIDER: GSE232537 | GEO | 2024/05/14

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (RNA-Seq)

Project description:To detect the mechanism underlying osteogenic commitment and proliferation rate change of HDPCs driven by MDL-800, we performed gene expression profiling analysis for HDPCs with DMSO or MDL-800 pre-treatment under normal or osteogenic differentiation conditions.

2024-05-14 | GSE232535 | GEO

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (ChIP-Seq)

Project description:To detect the mechanism underlying osteogenic commitment and proliferation rate change of HDPCs driven by MDL-800, we performed ChIP-seq analysis to detect the recruitment of genes on H3K9ac and H3K56ac in MDL-800 pre-treated HDPCs.

2024-05-14 | GSE232534 | GEO

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs

Project description:Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs

| PRJNA972682 | ENA

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (RNA-Seq)

Project description:Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (RNA-Seq)

| PRJNA972688 | ENA

Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (ChIP-Seq)

Project description:Cutting down steroid biosynthesis through SIRT6 induced H3K56ac deacetylation Fuels the osteogenic commitment of MSCs (ChIP-Seq)

| PRJNA972689 | ENA

Peptides and Pseudopeptides as SIRT6 Deacetylation Inhibitors.

Project description:SIRT6 belongs to the family of histone deacetylases (class III), but it also has mono-ADP-ribosyltransferase activity. SIRT6 is a nuclear sirtuin that has been associated with aging, cellular protection, and sugar metabolism. Despite these important roles for SIRT6, thus far, there are only a few weak SIRT6 inhibitors available, and no structure-activity relationship (SAR) studies have been published. This is the first study concerning peptides and pseudopeptides as SIRT6 deacetylation inhibitors and the first SAR data concerning SIRT6. We also investigated the molecular interactions using a homology model. We report three compounds exhibiting 62-91% SIRT6 inhibition at 200 ?M concentration. These compounds can serve as starting points for systematic SAR studies and SIRT6 inhibitor design.

| S-EPMC4025866 | biostudies-literature

Activation of SIRT6 Deacetylation by DNA Strand Breaks.

Project description:SIRT6 is an emerging regulator of longevity. Overexpression of SIRT6 extends the lifespan of mice. Conversely, SIRT6 knockout mice demonstrate severe metabolic defects and a shortened lifespan. The discrepancy between SIRT6's weak in vitro activity and robust in vivo activity has led to the hypothesis that this enzyme can be activated in response to DNA damage in cells. Here, we demonstrate that the deacetylase activity of SIRT6 can be stimulated by DNA strand breaks for synthetic peptide and histone substrates. The mechanism of activation is further explored by using an integrative chemical biology approach. SIRT6 can be preferentially activated by DNA lesions harboring a 5'-phosphate. The N- and C-termini of SIRT6 are strictly required for DNA break-induced activation. Additionally, the defatty-acylase activity of SIRT6 is also sensitive to DNA breaks, although the physiological significance needs further investigation. Collectively, our study sheds important light on the cellular regulation of diverse SIRT6 activities and suggests possible strategies for effective SIRT6 activation.

| S-EPMC10633859 | biostudies-literature

Human SIRT6 promotes DNA end resection through CtIP deacetylation.

Project description:SIRT6 belongs to the sirtuin family of protein lysine deacetylases, which regulate aging and genome stability. We found that human SIRT6 has a role in promoting DNA end resection, a crucial step in DNA double-strand break (DSB) repair by homologous recombination. SIRT6 depletion impaired the accumulation of replication protein A and single-stranded DNA at DNA damage sites, reduced rates of homologous recombination, and sensitized cells to DSB-inducing agents. We identified the DSB resection protein CtIP [C-terminal binding protein (CtBP) interacting protein] as a SIRT6 interaction partner and showed that SIRT6-dependent CtIP deacetylation promotes resection. A nonacetylatable CtIP mutant alleviated the effect of SIRT6 depletion on resection, thus identifying CtIP as a key substrate by which SIRT6 facilitates DSB processing and homologous recombination. These findings further clarify how SIRT6 promotes genome stability.

| S-EPMC3276839 | biostudies-literature

Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6.

Project description:The protein deacetylase SIRT6 maintains cellular homeostasis through multiple pathways that include the deacetylation of histone H3 and repression of transcription. Prior work suggests that SIRT6 is associated with chromatin and can substantially reduce global levels of H3 acetylation, but how SIRT6 is able to accomplish this feat is unknown. Here, we describe an exquisitely tight interaction between SIRT6 and nucleosome core particles, in which a 2:1 enzyme:nucleosome complex assembles via asymmetric binding with distinct affinities. While both SIRT6 molecules associate with the acidic patch on the nucleosome, we find that the intrinsically disordered SIRT6 C-terminus promotes binding at the higher affinity site through recognition of nucleosomal DNA. Together, multivalent interactions couple productive binding to efficient deacetylation of histones on endogenous chromatin. Unique among histone deacetylases, SIRT6 possesses the intrinsic capacity to tightly interact with nucleosomes for efficient activity.

| S-EPMC7568541 | biostudies-literature

Trichostatin A inhibits deacetylation of histone H3 and p53 by SIRT6.

Project description:SIRT6 is an epigenetic modification enzyme that regulates gene transcription through its deacetylase activity. In addition to histone protein, SIRT6 also modify other proteins and enzymes, some of which are central players in metabolic reprogramming and aging process. Therefore, SIRT6 has emerged as a therapeutic target for the treatment of metabolic disorder and age-related diseases. Here, we report that SIRT6 deacetylates lysine 382 of p53 in short synthetic peptide sequence and in full length p53. Further studies showed that the deacetylation of H3K9Ac and p53K382Ac are insensitive to nicotinamide inhibition, but are sensitive to trichostatin A (TSA) inhibition. Detailed kinetic analysis revealed that TSA competes with the peptide substrate for inhibition, and this inhibition is unique to SIRT6 in the sirtuin family. Taken together, this study not only suggests potential roles of SIRT6 in regulating apoptosis and stress resistance via direct deacetylation of p53, but also provides lead compound for the development of potent and selective SIRT6 inhibitors.

| S-EPMC5762261 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data