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PRMT5-interacting proteins detected in Hey cells LC–MS

ABSTRACT: Our previous results indicated that PRMT5 is involved in CDDP resistance and may be regulated by phosphorylation modification. To further explore the mechanism of PRMT5 involved in CDDP resistance, PRMT5-interacting proteins were screened for potential PRMT5 kinases by mass spectrometry.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Malignant Neoplasm Of Ovary

SUBMITTER: Ronghui Zhong

LAB HEAD: Tianzhi huang

PROVIDER: PXD061397 | Pride | 2025-03-06

REPOSITORIES: Pride

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			Action	DRS
	DataAnalysis.Method	Other
	LC-MS_PRMT5-interacting-proteins.xlsx	Xlsx
	SampleInfo.xml	Xml
	analysis.tdf	Other
	analysis.tdf_bin	Other

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Identification of PRMT5 phosphorylation sites in Hey cells LC-MS

Project description:Previous studies have shown that PRMT5 undergoes various PTMs, including phosphorylation and arginine methylation. In our investigation of PRMT5's PTMs, we detected elevated phospho-Ser/Thr levels of PRMT5 in CDDP-resistant ovarian cancer cells Hey compared to their parental counterparts by co-immunoprecipitation of PRMT5. To further identify the phosphorylation sites that may be involved in the CDDP resistance mechanism, we identified the phosphorylation modification sites of PRMT5 by mass spectrometry.

2025-03-06 | PXD061400 | Pride

PRMT5-interacting proteins detected in Hey cells LC–MS

Project description:Through previous studies, we found that PRMT5 is regulated by phosphorylation modification and thus participates in tumor drug resistance. To further explore the mechanism of PRMT5 resistance, we screened potential PRMT5 kinases by mass spectrometry of proteins interacting with PRMT5

2025-02-22 | PXD058763 | Pride

Identification of METTL3 arginine methylation sites in CDDP-resistant Hey cells LC-MS

Project description:Previous studies have shown that nuclear localization of METTL3 is associated with CDDP resistance. To identify key PTMS involved in the nuclear localization of METTL3 in CDDP-resistant ovarian cancer cells, we assessed the global methylation of arginine, as well as METTL3 phosphorylation, acetylation, O-GlcNAcylation, and crotonylation in CDDP-resistant and parental ovarian cancer cells. The results showed that arginine methylation of METTL3 was increased in CDDP-resistant cell lines. To further identify the arginine methylation sites that may be involved in the METTL3 resistance mechanism, we identified the methylation modification sites of METTL3 by mass spectrometry.

2025-03-06 | PXD061401 | Pride

Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery (RNA-Seq)

Project description:Protein Arginine MethylTransferase 5 (PRMT5) is known to mediate epigenetic control on chromatin and to functionally regulate components of the splicing machinery. In this study we show that selective deletion of PRMT5 in different organs leads to cell cycle arrest and apoptosis. At the molecular level, PRMT5 depletion results in reduced methylation of Sm proteins, aberrant constitutive splicing and in the Alternative Splicing (AS) of specific mRNAs. We identify Mdm4 as one of these mRNAs, which due to its weak 5’-Donor site, acts as a sensor of splicing defects and transduces the signal to activate the p53 response, providing a mechanistic explanation of the phenotype observed in PRMT5 conditional knockout mice. Our data demonstrate a key role of PRMT5, together with p53, as guardians of the transcriptome. This will have fundamental implications in our understanding of PRMT5 activity, both in physiological conditions, as well as pathological conditions, including cancer and neurological diseases. Total RNA was extracted from control and Prmt5 depleted Neural Stem/Progenitors Cells (NPCs) and Mouse Embryonic Fibroblasts (MEFs). Prmt5 depleted cells were treated with 4-OHT 24 hours before splitting to induce PRMT5 knockout and final libraries were sequenced in triplicates on Illumina HiSeq 2000.

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PRMT5 protects genomic integrity during global DNA demethylation in primordial germ cells and preimplantation embryos

Project description:Primordial germ cells (PGCs) and preimplantation embryos undergo epigenetic reprogramming, which entails comprehensive erasure of DNA methylation. We found that PRMT5, an arginine methyltransferase, translocates from the cytoplasm to the nucleus during this process. Here we show that conditional loss of PRMT5 in early PGCs caused complete male and female sterility, which is preceded by upregulation of LINE1 and IAP transposons and DNA damage response. Similarly, loss of maternal-zygotic PRMT5 also leads to IAP upregulation and early embryonic lethality. We detected the PRMT5-catalysed repressive H2A/H4R3me2s modification on LINE1 and IAP in early wildtype PGCs, directly implicating this mark in the maintenance of transposon silencing during DNA hypomethylation. PRMT5 subsequently translocates back to the cytoplasm of PGCs to participate in the previously described PIWI-interacting RNA (piRNA) pathway that promotes transposon silencing via de novo DNA re-methylation. Thus, PRMT5 has a novel direct role in genome defense during preimplantation development and in PGCs at the time of global DNA demethylation PGCs mRNA profiles of embryonic day 11.5 dpc control (Blimp1Cre;Prmt5flox/+) and Prmt5 germ cell knockout (Blimp1Cre;Prmt5 flox/flox) were generated by deep sequencing (SOLiD next generation sequencing).

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PRMT5 protects genomic integrity during global DNA demethylation in primordial germ cells and preimplantation embryos

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2016-05-19 | E-GEOD-75215 | biostudies-arrayexpress

A complex of C9ORF72 and p62 uses arginine methylation to eliminate stress granules by autophagy - PART 3

Project description:Mutations in proteins like FUS which cause Amyotrophic Lateral Sclerosis (ALS) result in the aberrant formation of stress granules while ALS-linked mutations in other proteins impede elimination of stress granules. Repeat expansions in C9ORF72, the major cause of ALS, reduce C9ORF72 levels but how this impacts stress granules is uncertain. Here, we demonstrate that C9ORF72 associates with the autophagy receptor p62 and controls elimination of stress granules by autophagy. This requires p62 to associate via the Tudor protein SMN with proteins, including FUS, that are symmetrically arginine-methylated by PRMT5. Mice lacking p62 accumulate arginine-methylated proteins and alterations in FUS-dependent splicing. Finally, patients with C9ORF72 repeat expansions accumulate symmetric arginine dimethylated proteins which co-localize with p62. This suggests that C9ORF72 initiates a cascade of ALS-linked proteins (C9ORF72, p62, SMN, FUS) to recognize stress granules for degradation by autophagy and hallmarks of a defect in this process are observable in ALS patients.

2018-07-25 | PXD009760 | Pride

Protein arginine methyltransferase 5 (PRMT5) is an actionable therapeutic target in CDK4/6 inhibitor-resistant ER+/RB-deficient breast cancer

Project description:PRMT5 Co-IP mass spectrometry: Lysates of MCF-7 RB1-knockout cells were pulled down with a PRMT5 antibody or IgG control. The pulldowns were subjected to mass spectrometry analysis. QEX2_981005, QEX2_981006, QEX2_981007: DMSO, IgG QEX2_981008, QEX2_981009, QEX2_981010: DMSO, PRMT5 antibody QEX2_981011, QEX2_981012, QEX2_981013, GSK, IgG QEX2_981014, QEX2_981015, QEX2_981016, GSK, PRMT5 antibody SDMA PTM analysis: MCF-7 RB1-knockout cells were transfected with a PRMT5 siRNA or a control siRNA. Lysates were collected three days after transfection and subjected to mass spectrometry analysis. LUM1_1000791, LUM1_1000792, LUM1_1000793: control SiRNA LUM1_1000794, LUM1_1000795, LUM1_1000796: PRMT5 siRNA [

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Genome-wide analysis of genes regulated by p44/wdr77 and PRMT5 in lung and prostate cancer cells

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