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Article

Arginine-rich C9ORF72 ALS proteins stall ribosomes in a manner distinct from a canonical ribosome-associated quality control substrate.

The Journal of biological chemistry - 1 Jan 2023

Kriachkov Viacheslav, Ormsby Angelique R, Kusnadi Eric P, McWilliam Hamish E G, Mintern Justine D, Amarasinghe Shanika L, Ritchie Matthew E, Furic Luc, Hatters Danny M

Abstract excerpt

Hexanucleotide expansion mutations in C9ORF72 are a frequent cause of amyotrophic lateral sclerosis. We previously reported that long arginine-rich dipeptide repeats (DPRs), mimicking abnormal proteins expressed from the hexanucleotide expansion, caused translation stalling when expressed in cell culture models. Whether this stalling provides a mechanism of pathogenicity remains to be determined. Here, we...

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Identifiers

PMID: 36481270
DOI: 10.1016/j.jbc.2022.102774
PMCID: PMC9830226

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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