ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
Dang Mei et al. use NMR and microscopy approaches to examine how ATP impacts the liquid-liquid phase separation (LLPS) of prion-like domains in TDP-43, a RNA-binding protein that is implicated in ALS and other neurological disorders. Their results suggest that ATP specifically binds to a subset of T...
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| Autores principales: | , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/f4adf49a14ff4b13b8c5014276353840 |
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| Sumario: | Dang Mei et al. use NMR and microscopy approaches to examine how ATP impacts the liquid-liquid phase separation (LLPS) of prion-like domains in TDP-43, a RNA-binding protein that is implicated in ALS and other neurological disorders. Their results suggest that ATP specifically binds to a subset of TDP-43 arginine residues at a particular molar ratio to modulate LLPS, and provides insight into how ATP affects the LLPS of biomolecular systems. |
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