Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?

Oxidative Stress in the Pathogenesis of Aorta Diseases as a Source of Potential Biomarkers and Therapeutic Targets, with a Particular Focus on Ascending Aorta Aneurysms

“…Concerning the expression of genes, RNA-binding proteins (RBP) have a key role in RNA expression and metabolism. Consequently, the appropriate control of these proteins is critical for cellular health [ 107 ]. Use of a clustered regularly interspaced short palindromic repeats (CRISPR)-Cas9-single guide RNA library and stimulation of cells with paraquat has permitted us to identify CSDE1 and STRAP proteins, which interact with each other and produce sensitivity to OS, and the Pumilio homologues (PUM1 and PUM2), which produce resistance [ 98 ].…”

“…Thus, this study emphasized that the use of genetic screening may allow us to identify RBPs and novel genes regulating the sensitivity to OS. They may be used for developing targeted treatments for OS [ 107 ].…”

“…Another class of novel OS regulators is the circular RNAs (circRNAs) [ 107 , 108 ], endogenous non-coding RNAs characterized by a covalently closed-loop structure generated through a special type of alternative splicing termed back-splicing. At this time, growing evidence has disclosed that circRNAs are evolutionarily conserved across species, stable and resistant to RNase R degradation.…”

Editorial: The Role of Protein Post-Translational Modifications in Protein-RNA Interactions and RNP Assemblies

“…The most well characterized PTMs of RBPs are phosphorylation, methylation, acetylation, sumoylation and ubiquitinylation. The first four of these PTMs have been mainly linked to the regulation of RBPs cellular distribution and interactions, while ubiquitinylation is mainly involved in protein degradation and turnover (Sternburg et al, 2022). Recently, all of these PTMs have been described to regulate the LLPS behavior of RBPs and the consequent formation of membraneless-organelles (MLOs), such as stress granules (SGs) or other ribonucleoprotein (RNP) granules (Wiedner and Giudice, 2021).The goal of our research topic is to highlight how PTMs regulate RNA-protein interactions, protein-protein interactions, LLPS of RBPs, and RNP granule formation and dynamics, as well as how altered PTM patterns on RBPs can be linked to human diseases.The review by Velázquez-Cruz et al summarizes the impact that PTMs have on several mammalian RBPs and how an aberrant PTM profile causes an alteration of physiological processes leading to diseases, such as cancer and neurodegenerative disorders.…”

“…The most well characterized PTMs of RBPs are phosphorylation, methylation, acetylation, sumoylation and ubiquitinylation. The first four of these PTMs have been mainly linked to the regulation of RBPs cellular distribution and interactions, while ubiquitinylation is mainly involved in protein degradation and turnover ( Sternburg et al, 2022 ). Recently, all of these PTMs have been described to regulate the LLPS behavior of RBPs and the consequent formation of membraneless-organelles (MLOs), such as stress granules (SGs) or other ribonucleoprotein (RNP) granules ( Wiedner and Giudice, 2021 ).…”