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Identification of PRMT1 interaction proteins in cancer and neural stem cells

ABSTRACT: We have showed that cancer cells (or tumorigenic cells) resemble neural stem/progenitor cells in regulatory network, tumorigenicity and differentiation potential. We have shown PRMT1 is a protein that is upreguated in and promotes vaious cancers. The expression of its gene is localized to embryonic neural cells during vertebrate embryogenesis. The project is to identify the interaction partners of PRMT1, by which PRMT1 regulates neural stemness in both cancer cells and neural stem cells.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Ying Cao

LAB HEAD: Ying Cao

PROVIDER: PXD026851 | Pride | 2021-12-20

REPOSITORIES: Pride

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			Action	DRS
	20190727_13.wiff	Wiff
	20190727_13.wiff.scan	Wiff
	20190727_13_CY01_Mouse_ProteinSummary.txt	Txt
	20190727_14.wiff	Wiff
	20190727_14.wiff.scan	Wiff

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Publications

Coordinated regulation of the ribosome and proteasome by PRMT1 in the maintenance of neural stemness in cancer cells and neural stem cells.

Chen Lu L Zhang Min M Fang Lei L Yang Xiaoli X Cao Ning N Xu Liyang L Shi Lihua L Cao Ying Y

The Journal of biological chemistry 20211004 5

Previous studies suggested that cancer cells resemble neural stem/progenitor cells in regulatory network, tumorigenicity, and differentiation potential, and that neural stemness might represent the ground or basal state of differentiation and tumorigenicity. The neural ground state is reflected in the upregulation and enrichment of basic cell machineries and developmental programs, such as cell cycle, ribosomes, proteasomes, and epigenetic factors, in cancers and in embryonic neural or neural st ...[more]

PMID: 34619150

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Identification of Setdb1 interaction proteins in neural stem cells

Project description:Setdb1 is an epigenetic factors catalyzing modification of H3K9me3. Expression of its gene is localized to embryonic neural cells during vertebrate embryogenesis, suggesting its role in regulating neural stemness. The project is to identify the interaction partners of Setdb1, by which Setdb1 regulates neural stemness in neural stem cells.

2022-08-12 | PXD030453 | Pride

Neuronal-like differentiation of A549 cells in response to PRMT1 knockdown

Project description:Formerly we found that cancer-promoting factors, such as some typical epigenetic modification factors, are neural specific or enriched in embryonic neural cells, and play a key role in conferring the property of nerual stemness to cancer cells or in maintaining neural stemness in neural stem/progenitor cells. Our recent study demonstrated that PRMT1, a protein arginine methyltransferase, serves also to maintain neural stemness in either neural stem/progenitor cells or cancer cells. We used microarray to analyze global gene expression change in A549 cells after PRMT1 knockdown.

2020-12-09 | GSE162840 | GEO

Protein arginine methyltransferase PRMT1 is essential for palatogenesis

Project description:We report that neural crest-specific deletion of Prmt1 caused craniofacial malformations including cleft palate.

2019-09-01 | GSE114894 | GEO

Toxoplasma gondii arginine methyltransferase 1 (PRMT1) regulates parasite counting during tachyzoite cell division

Project description:PRMT1 is thought to be responsible for the majority of PRMT activity in Toxoplasma gondii, but its exact function is unknown. We generated T. gondii mutants lacking PRMT1 (∆prmt1) by deletion of the PRMT1 gene. ∆prmt1 parasites exhibit morphological defects during cell division and grow slowly, and this phenotype reverses in the complemented strain ∆prmt::PRMT1mRFP. PRMT1 localizes primarily in the cytoplasm with enrichment at the centrosome, and the strain lacking PRMT1 is unable to segregate progeny accurately. Unlike wild-type and complemented parasites, ∆prmt1 parasites have abnormal daughter buds, perturbed centrosome stoichiometry, and loss of synchronous replication. Whole genome expression profiling demonstrated differences in expression of cell cycle regulated genes in ∆prmt1 relative to the complemented ∆prmt1::PRMT1mRFP and parental wild-type strains, but these changes did not correlate with a specific block in cell cycle. Although PRMT1’s primary biological function was previously proposed to be methylation of histones, our genetic studies suggest that the most critical function of PRMT1 is within the centrosome as a regulator of daughter cell counting to assure the proper replication of the parasite. RNA samples were isolated in triplicates from RH-hxgprt parent strain (W), PRMT1 knockout (K) strain and PRMT1 knockout strain complemented with RFP-tagged PRMT1 protein (C). Parasites were grown for 32h at 37C. Samples were hybridized to the Toxoplasma gondii Affymetrix microarray (ToxoGeneChip: http://ancillary.toxodb.org/docs/Array-Tutorial.html). Hybridization data was preprocessed with Robust Multi-array Average (RMA) and normalized using per chip and per gene median polishing and analyzed using the software package GeneSpring GX (Agilent Technologies).

2015-09-18 | E-GEOD-73177 | biostudies-arrayexpress

MStern Blot vs. FASP - Different sample types

Project description:Three different sample types (HeLa lysate, human CSF and human Urine) that were prepared with MStern Blot and FASP. For each sample type there are four replicates.

2015-07-30 | PXD002572 | Pride

Targeting epigenetic networks mediated by Prmt1 and Kdm4c in acute myeloid leukemia

Project description:Transcriptional deregulation plays a major role in acute myeloid leukemia, identification of epigenetic modifying enzymes essential for the maintenance of oncogenic transcription programs holds the key to better understanding the biology and designing effective therapeutic strategies for the disease. Here we provide experimental evidence showing the functional involvement and therapeutic potentials of targeting PRMT1 with H4R3 methyltransferase activity in various MLL and non-MLL leukemias. PRMT1 is necessary but not sufficient for leukemic transformation, which requires co-recruitment of KDM4C with H3K9 demethylase activity by chimeric transcription factors to mediate epigenetic reprogramming. Inhibition of KDM4C/PRMT1 suppresses transcription and transformation ability of MLL fusions and MOZ-TIF2, revealing a novel and targetable epigenetic circuitry mediated by PRMT1 and KDM4C in acute leukemia.

2016-01-14 | E-MTAB-3322 | biostudies-arrayexpress

PRMT1 and CSNK1a1 control epidermal progenitor maintanence (PRMT1 ChIP-seq data set)

Project description:Here we determine the genome-wide binding sites of PRMT1 in primary human keratinocytes. We also investigated the impact of casein kinase inhibitor D4476 on PRMT1 genomic binding.

2018-02-02 | GSE110050 | GEO

PRMT1 suppresses anti-tumor immunity

Project description:PRMT1 is known as a regulator of immune function by directly interacting with interferon receptors, methylating STAT1, and promoting B cell and macrophage differentiation by methylating CDK4 or B cell antigen receptor However, the function of PRMT1 as a therapeutic target of cancer remains largely elusive, particularly for its role in cancer immunosurveillance. Here, we performed bulk RNA-seq for CT26, a mouse tumor cell line, after either knocking down of endogeneous Prmt1 or blocking PRMT1 by two specific inhibitors, namely MS023 and GSK3368715.

2023-03-21 | GSE203466 | GEO

Prmt1-mediated translation regulation is a crucial vulnerability of cancer

Project description:Through an shRNA screen we have identified Prmt1 as a genetic vulnerability of p53/Rb-null murine osteosarcoma cells. Depletion of Prmt1 in p53-deficient cells impairs tumor initiation and maintenance in vitro and in vivo. Mechanistic studies reveal that translation-associated pathways are enriched for Prmt1 downstream targets, implicating a role of Prmt1 in translation control. In particular, we have shown that loss of Prmt1 leads to a the decrease in arginine methylation of the translation initiation complex, thereby disrupting its assembly and inhibiting translation. We also observed that p53/Rb-null cells are sensitive to p53-induced translation stress. Analysis of the human tumor cell Achilles data set further reveals that Prmt1 and translation-associated pathways converge on the same functional networks. We propose that targeted therapy directed to inhibition of Prmt1 and its associated translation-related pathways represents a novel and promising therapeutic strategy for p53-deficient cancer cells that exhibit dependencies on translation stress response.

2018-01-06 | GSE93309 | GEO

PRMT1 interacts with leukemia fusion protein AML1-ETO for activation of transcription and transformation

Project description:Fusion protein AML1-ETO resulted from t(8;21) translocation is highly related to leukemia development. We have previously shown that the expression of AE9a, a spliced form of AML1-ETO, can rapidly cause leukemia in mouse. To understand how AML1-ETO is involved in leukemia development, we used AE9a leukemia model to identify a novel AE9a interacting proteins PRMT1 (protein arginine methyltransferase 1) from primary leukemic cells expressing AE9a. To examine whether PRMT1 is involved in AE9a-mediated transcription regulation, genome wide gene expression analysis is carried out in hematopoietic cell line K562 (wild type or AE9a expressing) treated with (-) control siRNA or siPRMT1. Wild type or AE9a-expressing K562 cells with control siRNA or siPRMT1 in triplicate

2012-06-17 | E-GEOD-28135 | biostudies-arrayexpress

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