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- W3136258516 abstract "Hexanucleotide repeat expansion (G4C2 n ) mutations in the gene C9ORF72 account for approximately 30% of familial cases of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), as well as approximately 7% of sporadic cases of ALS. G4C2 n mutations are known to result in the production of five species of dipeptide repeat proteins (DRPs) through non-canonical translation processes. Arginine-enriched dipeptide repeat proteins, glycine-arginine (polyGR), and proline-arginine (polyPR) have been demonstrated to be cytotoxic and deleterious in multiple experimental systems. Recently, we and others have implicated methylation of polyGR/polyPR arginine residues in disease processes related to G4C2 n mutation-mediated neurodegeneration. We previously reported that inhibition of asymmetric dimethylation (ADMe) of arginine residues is protective in cell-based models of polyGR/polyPR cytotoxicity. These results are consistent with the idea that PRMT-mediated arginine methylation in the context of polyGR/polyPR exposure is harmful. However, it remains unclear why. Here we discuss the influence of arginine methylation on diverse cellular processes including liquid-liquid phase separation, chromatin remodeling, transcription, RNA processing, and RNA-binding protein localization, and we consider how methylation of polyGR/polyPR may disrupt processes essential for normal cellular function and survival." @default.
- W3136258516 created "2021-03-29" @default.
- W3136258516 creator A5005113764 @default.
- W3136258516 creator A5005231504 @default.
- W3136258516 creator A5040195959 @default.
- W3136258516 date "2021-03-23" @default.
- W3136258516 modified "2023-09-25" @default.
- W3136258516 title "Hypothesis and Theory: Roles of Arginine Methylation in C9orf72-Mediated ALS and FTD" @default.
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