Dual role of PRMT1-dependent arginine methylation in cellular responses to genotoxic stress

Giambruno, Roberto; Bonaldi, Tiziana

doi:10.1080/23723556.2020.1743808

Cited by 6 publications

(3 citation statements)

References 10 publications

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“…In fact, in addition to phosphorylating and redirecting PRTM1 toward chromatin, DNA-PK phosphorylates the RBPs that are a target of R-methylation in a way that inhibits their interaction with PRTM1. The net effect is that these RBPs accumulate in SG condensates ( Giambruno and Bonaldi, 2020 ). In the case of hnRNP-A2, Tyr-phosphorylation alters the propensity of the protein to undergo LLPS in vitro , prevents partitioning of granule components and hinders aggregation of mutants associated with neurodegenerative disorders.…”

Section: Post-translational Modifications Of Tdp-43 Fus and Hnrnp-a1 Controlling Liquid-liquid Phase Separation And Protein Aggregationmentioning

confidence: 99%

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Farina

Esposito

Battistoni

et al. 2021

Front. Mol. Biosci.

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It has been shown that protein low-sequence complexity domains (LCDs) induce liquid-liquid phase separation (LLPS), which is responsible for the formation of membrane-less organelles including P-granules, stress granules and Cajal bodies. Proteins harbouring LCDs are widely represented among RNA binding proteins often mutated in ALS. Indeed, LCDs predispose proteins to a prion-like behaviour due to their tendency to form amyloid-like structures typical of proteinopathies. Protein post-translational modifications (PTMs) can influence phase transition through two main events: i) destabilizing or augmenting multivalent interactions between phase-separating macromolecules; ii) recruiting or excluding other proteins and/or nucleic acids into/from the condensate. In this manuscript we summarize the existing evidence describing how PTM can modulate LLPS thus favouring or counteracting proteinopathies at the base of neurodegeneration in ALS.

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Section: Post-translational Modifications Of Tdp-43 Fus and Hnrnp-a1 Controlling Liquid-liquid Phase Separation And Protein Aggregationmentioning

confidence: 99%

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Farina

Esposito

Battistoni

et al. 2021

Front. Mol. Biosci.

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“…2). PRMT1 protein regulates multiple stress response pathways 40,41 , which have a roll in acute sleep loss.…”

Section: Resultsmentioning

confidence: 99%

Sleep and diurnal alternative polyadenylation sites associated with human APA-linked brain disorders

Flores,

Pasetto,

Wang

et al. 2024

Preprint

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Disruption of sleep and circadian rhythms are a comorbid feature of many pathologies, and can negatively influence many health conditions, including neurodegenerative disease, metabolic illness, cancer, and various neurological disorders. Genetic association studies linking sleep and circadian disturbances with disease susceptibility have mainly focused on changes in gene expression due to mutations, such as single-nucleotide polymorphisms. The interaction between sleep and/or circadian rhythms with the use of Alternative Polyadenylation (APA) has been largely undescribed, particularly in the context of other disorders. APA is a process that generates various transcript isoforms of the same gene affecting its mRNA translation, stability, localization, and subsequent function. Here we identified unique APAs expressed in rat brain over time-of-day, immediately following sleep deprivation, and the subsequent recovery period. From these data, we performed a secondary analysis of these sleep- or time-of-day associated PASs with recently described APA-linked human brain disorder susceptibility genes.

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“…PRMT1 was also reported to be involved in ovarian cancer cisplatin. PRMT1 arginine methylation controlled the response to cisplatin in ovarian cancer cells [ 54 ]. The inhibition of PRMT1 suppressed the cancer cells' growth when exposed to low doses of cisplatin, which sensitized them to apoptosis [ 55 ].…”

Section: Discussionmentioning

confidence: 99%

Methylation of BRD4 by PRMT1 regulates BRD4 phosphorylation and promotes ovarian cancer invasion

Liu,

et al. 2023

Cell Death Dis

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Bromodomain-containing protein 4 (BRD4), the major component of bromodomain and extra-terminal domain (BET) protein family, has important functions in early embryonic development and cancer development. However, the posttranslational modification of BRD4 is not well understood. Multiple approaches were used to explore the mechanism of PRMT1-mediated BRD4 methylation and to determine the biological functions of BRD4 and PRMT1 in ovarian cancer. Here we report that BRD4 is asymmetrically methylated at R179/181/183 by PRMT1, which is antagonized by the Jumonji-family demethylase, JMJD6. PRMT1 is overexpressed in ovarian cancer tissue and is a potential marker for poor prognosis in ovarian cancer patients. Silencing of PRMT1 inhibited ovarian cancer proliferation, migration, and invasion in vivo and in vitro. PRMT1-mediated BRD4 methylation was found to promote BRD4 phosphorylation. Compared to BRD4 wild-type (WT) cells, BRD4 R179/181/183K mutant-expressing cells showed reduced ovarian cancer metastasis. BRD4 arginine methylation is also associated with TGF-β signaling. Our results indicate that arginine methylation of BRD4 by PRMT1 is involved in ovarian cancer tumorigenesis. Targeting PRMT1-mediated arginine methylation may provide a novel diagnostic target and an effective therapeutic strategy for ovarian cancer treatment.

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Dual role of PRMT1-dependent arginine methylation in cellular responses to genotoxic stress

Cited by 6 publications

References 10 publications

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Sleep and diurnal alternative polyadenylation sites associated with human APA-linked brain disorders

Methylation of BRD4 by PRMT1 regulates BRD4 phosphorylation and promotes ovarian cancer invasion

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