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

Sternburg, Erin L. ; Gruijs da Silva, Lara A. ; Dormann, Dorothee

Trends in biochemical sciences (Amsterdam. Regular ed.), 2022-01, Vol.47 (1), p.6-22 [Periódico revisado por pares]

England: Elsevier Ltd

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Título:
Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?
Autor: Sternburg, Erin L. ; Gruijs da Silva, Lara A. ; Dormann, Dorothee
Assuntos: amyotrophic lateral sclerosis (ALS) ; Amyotrophic Lateral Sclerosis - genetics ; Amyotrophic Lateral Sclerosis - metabolism ; Amyotrophic Lateral Sclerosis - pathology ; frontotemporal dementia (FTD) ; Frontotemporal Dementia - genetics ; Frontotemporal Dementia - metabolism ; Fused in sarcoma (FUS) ; Humans ; Protein Processing, Post-Translational ; RNA-binding protein (RBP) ; RNA-Binding Protein FUS - genetics ; RNA-Binding Proteins - metabolism ; TAR DNA-binding protein of 43 kDa (TDP-43)
É parte de: Trends in biochemical sciences (Amsterdam. Regular ed.), 2022-01, Vol.47 (1), p.6-22
Descrição: RNA-binding proteins (RBPs) are critical players in RNA expression and metabolism, thus, the proper regulation of this class of proteins is critical for cellular health. Regulation of RBPs often occurs through post-translational modifications (PTMs), which allow the cell to quickly and efficiently respond to cellular and environmental stimuli. PTMs have recently emerged as important regulators of RBPs implicated in neurodegenerative disorders, in particular amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here, we summarize how disease-associated PTMs influence the biophysical properties, molecular interactions, subcellular localization, and function of ALS/FTD-linked RBPs, such as FUS and TDP-43. We will discuss how PTMs are believed to play pathological, protective, or ambiguous roles in these neurodegenerative disorders. Research in recent years has begun to tackle the impact of post-translational modifications (PTMs) on neurodegenerative disease-associated RNA binding proteins, such as FUS and TDP-43.Alterations in arginine methylation of FUS and abnormal phosphorylation, acetylation, oxidation, nitrosylation, ubiquitination, and proteolytic cleavage of TDP-43 are observed in postmortem brains of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) patients.Changes in the PTM landscape of FUS and TDP-43 seen in ALS and FTD alter the biophysical properties, molecular interactions, subcellular localization, and function of FUS and TDP-43.Some disease-linked PTMs may accelerate the disease process (e.g., by promoting mislocalization or aberrant phase separation), whereas others may act as ‘brakes’, attempting to correct other primary cellular issues that occur earlier in disease.
Editor: England: Elsevier Ltd
Idioma: Inglês

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

Sternburg, Erin L. ; Gruijs da Silva, Lara A. ; Dormann, Dorothee

England: Elsevier Ltd

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