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MetabolomicsLKB1 inactivation elicits a NNMT-mediated methyl sink and confers dependence on PRMT5 in lung cancer
The protein arginine methyl transferase 5 (PRMT5) emerges as a therapeutic target in S-methyl-5'-thioadenosine phosphorylase (MTAP)-deleted cancers, where MTA accumulation partially inhibits its activity. However, It remains unclear whether other genetic alterations can dictate PRMT5 activity in can...
2026-04-30 | MTBLS14411 | MetaboLights
ProteomicsPRMT5-interacting proteins detected in Hey cells LC–MS
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.
ORGANISM(S): Homo sapiens (Human) 
2025-03-06 | PXD061397 | Pride
Prmt5 interacting proteins 
ProteomicsPRMT5-interacting proteins detected in Hey cells LC–MS
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
ORGANISM(S): Homo sapiens (Human) 
2025-02-22 | PXD058763 | Pride
Prmt5 interacting proteins 
TranscriptomicsProteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members
In germ cells, Piwi proteins interact with a specific class of small non-coding RNAs, piwi-interacting RNAs (piRNAs). Together, these form a pathway that represses transposable elements, thus safeguarding germ cell genomes. While basic models describe the operation of piRNA pathways, neither the pr...
ORGANISM(S): Mus musculus 
2009-07-25 | E-GEOD-17319 | biostudies-arrayexpress
ProteomicsPRMT5 interacting partners and substrates in oligodendrocyte lineage cells
The protein arginine methyl transferase PRMT5 is an enzyme expressed in oligodendrocyte lineage cells and responsible for the symmetric methylation of arginine residues on histone tails. Previous work from our laboratory identified PRMT5 as critical for myelination, due to its transcriptional regula...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2021-11-16 | MSV000088396 | MassIVE
UnknownPRMT5 Interacting Partners and Substrates in Oligodendrocyte Lineage Cells.
Not available
S-EPMC8968030 | biostudies-literature
Genomicsα-Synuclein promotes H4R3me2s through interacting with BAF-PRMT5 complex
α-Synuclein promotes H4R3me2s through interacting with BAF-PRMT5 complex
PRJNA949282 | ENA
TranscriptomicsRNA-seq analysis of 22Rv1 cells with PRMT5, MEP50, pICln knockdown
PRMT5 is a methyltransferase that catalyzes symmetric dimethylation of arginine residues in histones (H4R3, H3R8, H3R2, and H2AR3) to regulate transcription of target genes. While PRMT5 is generally considered an epigenetic repressor, recent evidence from our lab and others demonstrate that PRMT5 al...
ORGANISM(S): Homo sapiens 
2022-05-05 | GSE154951 | GEO
GenomicsRNA-seq analysis of 22Rv1 cells with PRMT5, MEP50, pICln knockdown
RNA-seq analysis of 22Rv1 cells with PRMT5, MEP50, pICln knockdown
PRJNA648043 | ENA
UnknownProtein Arginine Methyltransferase 5 Functions via Interacting Proteins.
Not available
S-EPMC8432624 | biostudies-literature
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