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Identification of PRMT5 phosphorylation sites in Hey cells LC-MS

ABSTRACT: 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.

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: PXD061400 | Pride | 2025-03-06

REPOSITORIES: pride

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			Action	DRS
	DataAnalysis.Method	Other
	LC-MS_Identification-PRMT5-phosphorylation-site.xlsx	Xlsx
	SampleInfo.xml	Xml
	analysis.tdf	Other
	analysis.tdf_bin	Other

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PRMT5-interacting proteins detected in Hey cells LC–MS

Project description: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.

2025-03-06 | PXD061397 | Pride

PRMT5-interacting proteins detected in Hey cells LC–MS

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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

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

Project description:Analysis of gene expression in lung and prostate cancer cells expressing non-target (NT), p44/wdr77. or PRMT5 shRNA. Results provide important information on how p44/wdr77 and PRMT5 control cellular proliferation. Total RNA obtained from cells expressing NT, p44/wdr77, or PRMT5 shRNA.

2014-04-14 | E-GEOD-56757 | biostudies-arrayexpress

Regulation of the core pre-mRNA splicing machinery by MYC and PRMT5 is essential to sustain lymphomagenesis [B-cells]

Project description:Over-expressed MYC binds to virtually all active promoters within a cell, although with different binding affinities, and modulates gene expression, both positively and negatively. Here, we show that during lymphomagenesis in Eµ-myc transgenic mice, MYC directly up-regulates the transcription of the core snRNP assembly genes, including PRMT5, an arginine methyltransferase, that methylates Sm proteins as an early step in lymphomagenesis. This coordinated regulatory effect is direct and is critical for snRNP biogenesis, the maintenance of effective mRNA splicing and cellular viability in cycling cells, in either fibroblasts or B-cells. mRNA profiles of wild type and pre-tumoral eu-myc mice by deep sequencing, in triplicate, using Illumina NextSeq 500

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The Sm protein methyltransferase PRMT5, is not required for primordial germ cell specification in mice

Project description:PRMT5 is a type II protein arginine methyltransferase with roles in stem cell biology, reprogramming, cancer and neurogenesis. During embryogenesis in the mouse it was hypothesized that PRMT5 functions with the master germline determinant BLIMP1 to promote primordial germ cell (PGC) specification. Using a Blimp1-Cre germline conditional knockout, we discovered that Prmt5 has no major role in murine germline specification, or the first global epigenetic reprogramming event involving depletion of cytosine methylation from DNA and histone H3 lysine 9 dimethylation from chromatin. Instead, we discovered that PRMT5 functions at the conclusion of PGC reprogramming I to promote proliferation, survival and expression of the gonadal germline program as marked by MVH. We show that PRMT5 regulates gene expression by promoting methylation of the Sm spliceosomal proteins, and significantly altering the spliced repertoire of RNAs in mammalian embryonic cells and primordial cells. Examination of transcriptional profile of iPHet (Control) vs. iPKO (Prmt5 knock out) 2i Embryonic Stem Cells

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