Poly-GR Impairs PRMT1-Mediated Arginine Methylation of Disease-Linked RNA-Binding Proteins by Acting as a Substrate Sink-Reference-Cited by-同舟云学术

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Poly-GR Impairs PRMT1-Mediated Arginine Methylation of Disease-Linked RNA-Binding Proteins by Acting as a Substrate Sink

Published:2024-08-15 Issue:17 Volume:63 Page:2141-2152
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hutten Saskia¹^ORCID,Chen Jia-Xuan²,Isaacs Adrian M.³⁴,Dormann Dorothee¹²

Affiliation:

1. Institute of Molecular Physiology, Johannes Gutenberg-Universität, 55128 Mainz, Germany

2. Institute of Molecular Biology, 55128 Mainz, Germany

3. UK Dementia Research Institute at UCL, London WC1E 6BT, U.K.

4. Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 3BG, U.K.

Funder

Fritz Thyssen Stiftung

Deutsche Forschungsgemeinschaft

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00308

Reference80 articles.

1. Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

2. A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

3. Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD

4. Heterogeneous ribonuclear protein A3 (hnRNP A3) is present in dipeptide repeat protein containing inclusions in Frontotemporal Lobar Degeneration and Motor Neurone disease associated with expansions in C9orf72 gene

5. hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations

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