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:	Mei Dang, Liangzhong Lim, Jian Kang, Jianxing Song
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f4adf49a14ff4b13b8c5014276353840
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spelling	oai:doaj.org-article:f4adf49a14ff4b13b8c50142763538402021-12-02T17:52:31ZATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues10.1038/s42003-021-02247-22399-3642https://doaj.org/article/f4adf49a14ff4b13b8c50142763538402021-06-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02247-2https://doaj.org/toc/2399-3642Dang 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.Mei DangLiangzhong LimJian KangJianxing SongNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Mei Dang Liangzhong Lim Jian Kang Jianxing Song ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
description	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.
format	article
author	Mei Dang Liangzhong Lim Jian Kang Jianxing Song
author_facet	Mei Dang Liangzhong Lim Jian Kang Jianxing Song
author_sort	Mei Dang
title	ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
title_short	ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
title_full	ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
title_fullStr	ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
title_full_unstemmed	ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
title_sort	atp biphasically modulates llps of tdp-43 pld by specifically binding arginine residues
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/f4adf49a14ff4b13b8c5014276353840
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ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues

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