Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response

The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.

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Autores principales:	Yi Yang, Thea L. Willis, Robert W. Button, Conor J. Strang, Yuhua Fu, Xue Wen, Portia R. C. Grayson, Tracey Evans, Rebecca J. Sipthorpe, Sheridan L. Roberts, Bing Hu, Jianke Zhang, Boxun Lu, Shouqing Luo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/63468e0902e8452ea56c0ff4e2ec70b3
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spelling	oai:doaj.org-article:63468e0902e8452ea56c0ff4e2ec70b32021-12-02T15:35:27ZCytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response10.1038/s41467-019-11671-22041-1723https://doaj.org/article/63468e0902e8452ea56c0ff4e2ec70b32019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11671-2https://doaj.org/toc/2041-1723The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.Yi YangThea L. WillisRobert W. ButtonConor J. StrangYuhua FuXue WenPortia R. C. GraysonTracey EvansRebecca J. SipthorpeSheridan L. RobertsBing HuJianke ZhangBoxun LuShouqing LuoNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-18 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yi Yang Thea L. Willis Robert W. Button Conor J. Strang Yuhua Fu Xue Wen Portia R. C. Grayson Tracey Evans Rebecca J. Sipthorpe Sheridan L. Roberts Bing Hu Jianke Zhang Boxun Lu Shouqing Luo Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
description	The autophagy protein p62 undergoes liquid-liquid phase separation but how this is regulated is unclear. Here, the authors report that the histone chaperone DAXX interacts with p62 in the cytoplasm to drive its phase separation.
format	article
author	Yi Yang Thea L. Willis Robert W. Button Conor J. Strang Yuhua Fu Xue Wen Portia R. C. Grayson Tracey Evans Rebecca J. Sipthorpe Sheridan L. Roberts Bing Hu Jianke Zhang Boxun Lu Shouqing Luo
author_facet	Yi Yang Thea L. Willis Robert W. Button Conor J. Strang Yuhua Fu Xue Wen Portia R. C. Grayson Tracey Evans Rebecca J. Sipthorpe Sheridan L. Roberts Bing Hu Jianke Zhang Boxun Lu Shouqing Luo
author_sort	Yi Yang
title	Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
title_short	Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
title_full	Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
title_fullStr	Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
title_full_unstemmed	Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response
title_sort	cytoplasmic daxx drives sqstm1/p62 phase condensation to activate nrf2-mediated stress response
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/63468e0902e8452ea56c0ff4e2ec70b3
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_version_	1718386536284684288

Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response

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