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Embryonic stem cell differentiation is regulated by SET through interactions with p53 and β‐catenin

ABSTRACT: Embryonic stem cell differentiation is regulated by SET through interactions with p53 and β‐catenin

PROVIDER: PRJNA646766 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12244518.fastq.gz	Fastqsanger.gz
	SRR12244519.fastq.gz	Fastqsanger.gz
	SRR12244520.fastq.gz	Fastqsanger.gz
	SRR12244521.fastq.gz	Fastqsanger.gz
	SRR12244522.fastq.gz	Fastqsanger.gz

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Embryonic stem cell differentiation is regulated by SET through interactions with p53 and β‐catenin

Project description:The multifunctional histone chaperone, SET, is essential for embryonic development in mouse. Previously, we identified SET as a factor that is rapidly downregulated during embryonic stem cell (ESC) differentiation, suggesting a possible role in the maintenance of pluripotency. Here, we set out to explore SET’s function and its mechanism in early differentiation. Using liquid chromatography tandem mass spectrometry (LC‐MS/MS), we uncover the factors and complexes, including P53 and β-catenin, by which SET regulates lineage-specification. SET knockout (KO) and shRNA-knockdown experiments for both P53 and β-catenin in SET-KO ESCs reveal that P53 knockdown partially rescues lineage-marker misregulation during differentiation. β-catenin depletion, on the other hand, rescues the elevated Wnt gene expression observed in SET-KO ESCs. Integration of multiple ChIP-seq and RNA-seq datasets reveals a predominantly activating function of SET in gene regulation. Moreover, further analysis reveals a co-regulatory relationship between SET and TCF3, a downstream effector of Wnt-signalling. Overall, we discover a role for both P53 and β-catenin in SET-regulated early differentiation and uncover a potential mechanism for SET function at the β-catenin-TCF regulatory axis.

2020-12-22 | GSE154607 | GEO

RNA-seq analysis to identify the genes regulated by p53-SET interplay

Project description:To identify the genes regulated by SET in a p53-dependent manner, the endogenous SET was depleted by siRNA in control or p53 knockout U2OS cells. Total RNA from each sample was extracted and the whole profile of gene expression was analyzed by RNA-seq analysis.

2016-09-12 | GSE83635 | GEO

Embryonic Stem Cell Differentiation Is Regulated by SET through Interactions with p53 and β-Catenin.

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p53 forms redox-dependent protein-protein interactions through cysteine 277

Project description:Reversible cysteine oxidation plays an essential role in redox signaling by reversibly altering protein structure and function. Cysteine oxidation may lead to intra- and intermolecular disulfide formation, and the latter can drastically stabilize protein-protein interactions in a more oxidizing milieu. The activity of the tumor suppressor p53 is regulated at multiple layers, including various post-translational modification (PTM) and protein-protein interactions. In the past decades, p53 has been shown to be a redox sensitive protein, and undergoes reversible cysteine oxidation both in vitro and in vivo. It is not clear however, whether p53 also forms intermolecular disulfides with interacting proteins and whether these redox-dependent interactions contribute to the regulation of p53. In the present study, by combining (co-)immunoprecipitation, quantitative Mass spectrometry and Western blot we found that p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions. p53-Cys277 is required for most of the disulfide-dependent interactions, including those with 14-3-3 and 53BP1. Taken together, our findings uncovered a new form of p53 cysteine oxidation, which strengthened the biochemical features of p53 as a redox sensitive protein.

2021-11-02 | PXD026893 | Pride

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Top-Down Individual Ion Mass Spectrometry Reveals 85-110 kDa Catenin Phospho-Proteoforms Regulated by Actomyosin Contractility

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