Post-Translational Modifications and RNA-Binding Proteins

2016 ◽  
pp. 297-317 ◽  
Author(s):  
Michael T. Lovci ◽  
Mario H. Bengtson ◽  
Katlin B. Massirer
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Post Translational Modifications

scholarly journals Understanding the Role of Post‐Translational Modifications on the Splicing Activity of RNA Binding Proteins

2018 ◽  
Vol 32 (S1) ◽  
Author(s):  
Niroshika M. Keppetipola ◽  
Jeffrey Pina ◽  
Janice Reynaga ◽  
Anthony Truong
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Post Translational Modifications

scholarly journals An Emerging Role for Post-translational Modifications in Regulating RNP Condensates in the Germ Line

2021 ◽  
Vol 8 ◽  
Author(s):  
Jennifer A. Schisa ◽  
Mohamed T. Elaswad
Keyword(s):  
Phase Separation ◽  
Binding Proteins ◽  
Rna Binding ◽  
Germ Line ◽  
Rna Binding Proteins ◽  
Model Systems ◽  
Subsequent Formation ◽  
Post Translational Modifications ◽  
Rnp Granules

RNA-binding proteins undergo regulated phase transitions in an array of cell types. The phase separation of RNA-binding proteins, and subsequent formation of RNP condensates or granules, occurs during physiological conditions and can also be induced by stress. Some RNP granules have roles in post-transcriptionally regulating mRNAs, and mutations that prevent the condensation of RNA-binding proteins can reduce an organism’s fitness. The reversible and multivalent interactions among RNP granule components can result in RNP complexes that transition among diffuse and condensed states, the latter of which can be pathological; for example, in neurons solid RNP aggregates contribute to disease states such as amyotrophic lateral sclerosis (ALS), and the dysregulation of RNP granules in human germ cells may be involved in Fragile X-associated primary ovarian insufficiency. Thus, regulating the assembly of mRNAs and RNA-binding proteins into discrete granules appears to provide important functions at both cellular and physiological levels. Here we review our current understanding of the role of post-translational modifications (PTMs) in regulating the condensation of RNA-binding proteins in the germ line. We compare and contrast the in vitro evidence that methylation inhibits phase separation of RNA binding proteins, with the extent to which these results apply to the in vivo germ line environment of several model systems. We also focus on the role of phosphorylation in modulating the dynamics of RNP granules in the germ line. Finally, we consider the gaps that exist in our understanding of the role of PTMs in regulating germ line RNP granules.

FMRP and MicroRNAs in Neuronal Protein Synthesis

2018 ◽  
Author(s):  
Monica C. Lannom ◽  
Stephanie Ceman
Keyword(s):  
Protein Synthesis ◽  
Binding Proteins ◽  
Neuronal Development ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Post Translational Modifications ◽  
Local Protein Synthesis ◽  
Recognition Element ◽  
Neuronal Protein ◽  
And Function

New protein synthesis is critical for learning and memory. The discovery of ribosomes at synapses indicated the potential for local protein synthesis in response to stimulation. miRNAs play a key role in this process as evidenced by their role in normal neuronal development and function and in neurological disease. miRNA production is regulated and once bound by AGO2, the ensuing RISC complex is able to bind mRNAs and direct their translation suppression and degradation. However, other RNA binding proteins, including FMRP and MOV10, regulate AGO2 association with the miRNA recognition element (MRE) in target mRNAs. AGO2 itself is regulated by post-translational modifications, and neuronal activity controls post-translational modifications of FMRP and MOV10 that lead to their regulation and degradation. In addition, RNA localization at the synapse is a critical regulated event that depends on both cis sequences in the mRNA and the identity of the bound RNA binding proteins.

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