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Surf4 facilitates reprogramming by activating the cellular response to ER stress

ABSTRACT: Surf4 facilitates reprogramming by activating the cellular response to ER stress

PROVIDER: PRJNA735221 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14735592_1.fastq.gz	Fastqsanger.gz
	SRR14735592_2.fastq.gz	Fastqsanger.gz
	SRR14735593_1.fastq.gz	Fastqsanger.gz
	SRR14735593_2.fastq.gz	Fastqsanger.gz
	SRR14735594_1.fastq.gz	Fastqsanger.gz

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Surf4 facilitates reprogramming by activating the cellular response to ER stress

Project description:By somatic cell nuclear transfer, the oocytes can reprogram terminally differentiated cells back to totipotent state. So the oocytes enriched maternal proteins attract great interests in exploring key factors in somatic cell reprogramming. Here, we presented a maternal factor, surfeit locus protein 4 (Surf4), can significantly facilitate the generation of induced pluripotent stem cells (iPSCs) in a proliferation-independent manner. When co-expressed with Oct4, Sox2, Klf4 and c-Myc (OSKM), Surf4 can activate the response to endoplasmic reticulum (ER) stress at early stage of reprogramming. Besides, blocking unfolded protein response (UPR) compromised the effect of Surf4 on reprogramming. In conclusion, Surf4 serves as an activator for somatic cell reprogramming by activating the response to ER stress.

2021-11-18 | GSE176177 | GEO

Pharmacologic IRE1/XBP1s Activation Confers Targeted ER Proteostasis Reprogramming

Project description:Activation of the IRE1/XBP1s signaling arm of the unfolded protein response (UPR) is a promising strategy to correct defects in endoplasmic reticulum (ER) proteostasis implicated in diverse diseases. However, no pharmacologic activators of this pathway identified to date are suitable for ER proteostasis remodeling through selective activation of IRE1/XBP1s signaling. Here, we use high-throughput screening to identify non-toxic compounds that induce ER proteostasis remodeling through IRE1/XBP1s activation. We employ transcriptional profiling to stringently confirm that our prioritized compounds selectively activate IRE1/XBP1s signaling without activating other cellular stress-responsive signaling pathways. Furthermore, we demonstrate that our compounds improve ER proteostasis of destabilized variants of amyloid precursor protein (APP) through an IRE1-dependent mechanism and reduce APP-associated mitochondrial toxicity in cellular models. These results establish highly-selective IRE1 activating compounds that can be widely employed to define the functional importance of IRE1/XBP1s activity for ER proteostasis regulation in the context of health and disease.

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Project description:This SuperSeries is composed of the following subset Series: GSE35775: The H3K27 demethylase Utx facilitates somatic and germ cell epigenetic reprogramming to pluripotency [Affymetrix gene expression] GSE37821: The H3K27 demethylase Utx facilitates somatic and germ cell epigenetic reprogramming to pluripotency [ChIP-Seq] Refer to individual Series

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Targeted H3R26 deimination specifically facilitates ER binding by modifying nucleosome structure

Project description:The precise mechanisms by which hormone receptors bind to DNA in the context of chromatin remain unclear. Here we report that the genomic distributions of estrogen receptor (ER) and H3R26 deimination (H3R26Cit) in breast cancer cells are strikingly coincident, linearly correlated, and observed as early as 2 minutes following estradiol treatment. Paired-end MNase ChIP-seq indicates that the charge-neutral H3R26Cit modification facilitates ER binding to DNA by altering the fine structure of the nucleosome. Clinically, we find that PAD2 and H3R26Cit levels correlate with ER expression in breast tumors and that high PAD2 expression is associated with increased survival in ER+ breast cancer patients. Our study suggests that PAD2-mediated histone deimination is fundamental to ER signaling in breast cancer. We performed replicate H3R26Cit ChIP-seq experiments prior to estrogen treatment and 2min, 5min, 10min, 40min, and 160min after E2 treatment. Additionally, we performed H3R26Cit and H3K27ac ChIP on MNase digested chromatin.

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Surf4 facilitates reprogramming by activating the cellular response to endoplasmic reticulum stress.

Project description:ObjectivesMaternal factors that are enriched in oocytes have attracted great interest as possible key factors in somatic cell reprogramming. We found that surfeit locus protein 4 (Surf4), a maternal factor, can facilitate the generation of induced pluripotent stem cells (iPSCs) previously, but the mechanism remains elusive.Materials and methodsIn this study, we investigated the function and mechanism of Surf4 in somatic cell reprogramming using a secondary reprogramming system. Alkaline phosphatase (AP) staining, qPCR and immunofluorescence (IF) staining of expression of related markers were used to evaluate efficiency of iPSCs derived from mouse embryonic fibroblasts. Embryoid body and teratoma formation assays were performed to evaluate the differentiation ability of the iPSC lines. RNA-seq, qPCR and western blot analysis were applied to validate the downstream targets of Surf4.ResultsSurf4 can significantly facilitate the generation of iPSCs in a proliferation-independent manner. When co-expressed with Oct4, Sox2, Klf4 and c-Myc (OSKM), Surf4 can activate the response to endoplasmic reticulum (ER) stress at the early stage of reprogramming. We further demonstrated that Hspa5, a major ER chaperone, and the active spliced form of Xbp1 (sXbp1), a major mediator of ER stress, can mimic the effects of Surf4 on somatic cell reprogramming. Concordantly, blocking the unfolded protein response compromises the effect of Surf4 on reprogramming.ConclusionsSurf4 promotes somatic cell reprogramming by activating the response to ER stress.

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Targeted H3R26 deimination specifically facilitates ER binding by modifying nucleosome structure

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Chromatin Open/Close Logic in Cellular Reprogramming

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NF1 deficiency drives metabolic reprogramming in ER+ breast cancer

Project description:NF1 deficiency drives metabolic reprogramming in ER+ breast cancer

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