Research Topic

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

About this Research Topic

Protein post-translational modifications (PTMs) modulate protein functions through modification of the chemical properties of amino acids. A multitude of PTMs, such as arginine methylation, phosphorylation, and acetylation, are known to regulate the interaction of RNA-binding proteins (RBPs) with different classes of RNAs and with other proteins. RBPs interact with RNAs through well-structured RNA-binding motifs, e.g. RNA recognition motifs (RRM), K-homology (KH) domains and double-stranded RNA-binding motifs (dsRBM). RNA-protein and protein-protein interactions occur at disordered RNA-binding motifs, such as the highly abundant RG/RGG, RS-rich and low-complexity regions. In particular, disordered RNA-binding motifs are frequently post-translationally modified, especially in response to environmental stress. The chemical changes imposed by PTMs can regulate the folding, motions or interactions of a disordered region; can directly influence protein-RNA and protein-protein interactions; and can modulate liquid-liquid phase separation (LLPS) of RBPs and the consequent formation or dissolution of ribonucleoprotein (RNP) granules.

The regulation of RBPs interactions through PTMs is important both in physiological conditions and in response to environmental stress or external stimuli. Altered PTMs, as well as genetic mutations in post-translationally modified amino acids of RBPs, are often linked to human diseases, such as neurodegenerative disorders and cancer. PTMs have also been recognized as key modulators of LLPS, and of the formation and dynamics of membrane-less organelles in cells, e.g. stress granules or other RNP granules consisting of RBPs and RNAs.

Despite numerous recent advances, several questions remain to be addressed to fully understand how PTMs regulate RNA-protein interactions, protein-protein interactions, RNA processing functions and phase separation of RBPs. For example: Which PTMs specifically regulate RNA-protein interactions and molecular functions of RBPs? Are disordered RNA-binding regions stably or transiently modified by PTMs? Is there a PTM code regulating RNA-protein interactions or RNA metabolic processes? Can we pharmacologically alter PTMs in RBPs? What are the consequences of disease-linked PTMs, do they have a pathological or rather a protective/compensatory function?

The goal of this Research Topic is to foster research in this emerging topic area and to create a platform for exchange of ideas, methods and opinions.

The Research Topic will focus on the impact that PTMs have on the molecular interactions between RBPs and RNAs, their functional consequences in cells and their pathological consequences in disease.
In particular, topics of interest include, but are not limited to:

• Impact of PTMs on RNA recognition and interactions of RBPs
• Liquid-Liquid phase separation of RNA-binding proteins
• Role of PTMs in ribonucleoprotein particles (RNPs) granule formation and dynamics
• Alteration of PTMs in RBPs and connection with cancer
• Deregulation of PTMs in RBPs and the link with neurodegenerative disorders (e.g. ALS, FTD)

Manuscripts, within the format of Frontiers, that will be considered include: Methods; Original Research; Brief Research Report; Review; Mini Review; and Opinion. A full list with descriptions can be found here.


Dr. Nicolas Lux Fawzi is a member of the Scientific Advisory Board of Dewpoint Therapeutics LLC. All other Topic Editors declare no competing interests with regards to the Research Topic.


Keywords: PTMs, RNA-protein interactions, RNP granules, phase separation, intrinsic disordered regions


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

Protein post-translational modifications (PTMs) modulate protein functions through modification of the chemical properties of amino acids. A multitude of PTMs, such as arginine methylation, phosphorylation, and acetylation, are known to regulate the interaction of RNA-binding proteins (RBPs) with different classes of RNAs and with other proteins. RBPs interact with RNAs through well-structured RNA-binding motifs, e.g. RNA recognition motifs (RRM), K-homology (KH) domains and double-stranded RNA-binding motifs (dsRBM). RNA-protein and protein-protein interactions occur at disordered RNA-binding motifs, such as the highly abundant RG/RGG, RS-rich and low-complexity regions. In particular, disordered RNA-binding motifs are frequently post-translationally modified, especially in response to environmental stress. The chemical changes imposed by PTMs can regulate the folding, motions or interactions of a disordered region; can directly influence protein-RNA and protein-protein interactions; and can modulate liquid-liquid phase separation (LLPS) of RBPs and the consequent formation or dissolution of ribonucleoprotein (RNP) granules.

The regulation of RBPs interactions through PTMs is important both in physiological conditions and in response to environmental stress or external stimuli. Altered PTMs, as well as genetic mutations in post-translationally modified amino acids of RBPs, are often linked to human diseases, such as neurodegenerative disorders and cancer. PTMs have also been recognized as key modulators of LLPS, and of the formation and dynamics of membrane-less organelles in cells, e.g. stress granules or other RNP granules consisting of RBPs and RNAs.

Despite numerous recent advances, several questions remain to be addressed to fully understand how PTMs regulate RNA-protein interactions, protein-protein interactions, RNA processing functions and phase separation of RBPs. For example: Which PTMs specifically regulate RNA-protein interactions and molecular functions of RBPs? Are disordered RNA-binding regions stably or transiently modified by PTMs? Is there a PTM code regulating RNA-protein interactions or RNA metabolic processes? Can we pharmacologically alter PTMs in RBPs? What are the consequences of disease-linked PTMs, do they have a pathological or rather a protective/compensatory function?

The goal of this Research Topic is to foster research in this emerging topic area and to create a platform for exchange of ideas, methods and opinions.

The Research Topic will focus on the impact that PTMs have on the molecular interactions between RBPs and RNAs, their functional consequences in cells and their pathological consequences in disease.
In particular, topics of interest include, but are not limited to:

• Impact of PTMs on RNA recognition and interactions of RBPs
• Liquid-Liquid phase separation of RNA-binding proteins
• Role of PTMs in ribonucleoprotein particles (RNPs) granule formation and dynamics
• Alteration of PTMs in RBPs and connection with cancer
• Deregulation of PTMs in RBPs and the link with neurodegenerative disorders (e.g. ALS, FTD)

Manuscripts, within the format of Frontiers, that will be considered include: Methods; Original Research; Brief Research Report; Review; Mini Review; and Opinion. A full list with descriptions can be found here.


Dr. Nicolas Lux Fawzi is a member of the Scientific Advisory Board of Dewpoint Therapeutics LLC. All other Topic Editors declare no competing interests with regards to the Research Topic.


Keywords: PTMs, RNA-protein interactions, RNP granules, phase separation, intrinsic disordered regions


Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.

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Submission Deadlines

25 September 2020 Abstract
29 January 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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Topic Editors

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Submission Deadlines

25 September 2020 Abstract
29 January 2021 Manuscript

Participating Journals

Manuscripts can be submitted to this Research Topic via the following journals:

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