Author(s)
Mona Radwan
Published 2 Projects
Biochemistry Protein Aggregation Enriched Go Terms Gocc Gopb Methylosome
Ching-Seng Ang
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Biochemistry Protein Aggregation Enriched Go Terms Gocc Gopb Methylosome
Angelique R. Ormsby
Published 3 Projects
Biochemistry Cell Biology Protein Aggregation Methylosome Abce1
Gavin E. Reid
Published 3 Projects
Metabolism Biochemistry Protein Aggregation Proteasome Protein Homeostasis
Danny Hatters
Published 4 Projects
Metabolism Biochemistry Cell Biology Protein Aggregation Proteasome
Content
Video Abstract (AI generated) (01:34) Paper PreprintC9ORF72-associated Motor Neuron Disease patients feature abnormal expression of 5 dipeptide repeat (DPR) polymers. Here we used quantitative proteomics in a Neuro2a cell model to demonstrate that the valency of Arg in the most toxic DPRS, PR and GR, drives promiscuous binding to the proteome, compared to a relative sparse binding of the more inert AP and GA. Notable targets included ribosomal proteins, translation initiation factors and translation elongation factors. PR and GR comprising more than 10 repeats robustly stalled the ribosome suggesting high-valency Arg electrostatically jams the ribosome exit tunnel during synthesis. Poly-GR also bound to arginine methylases and induced hypomethylation of endogenous proteins, with a profound destabilization of the actin cytoskeleton. Our findings point to arginine in GR and PR polymers as multivalent toxins to translation as well as arginine methylation with concomitant downstream effects on widespread biological processes including ribosome biogenesis, mRNA splicing and cytoskeleton assembly.
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Danny Hatters. (2021, Nov 1).Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins[Video]. Scitok. https://scitok.com/project/p/41ca6c91
Radwan Mona. "Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins" Scitok, uploaded by Hatters Danny, 1 Nov, 2021, https://scitok.com/project/p41ca6c91
Danny Hatters. "Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins" Scitok. (Nov 1, 2021). https://scitok.com/project/p/41ca6c91
Danny Hatters (Nov 1, 2021). Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins Scitok. https://scitok.com/project/p/41ca6c91
Danny Hatters. Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins[video]. 2021 Nov 1. https://scitok.com/project/p/41ca6c91
@online{al2006link, title={ Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins }, author={ Hatters, Danny }, organization={Scitok}, month={ Nov }, day={ 1 }, year={ 2021 }, url = {https://scitok.com/project/p/41ca6c91}, }