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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):

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.

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PRMT5-interacting proteins detected in Hey cells LC–MS

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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.

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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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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]

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