Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes

Pathogen triggered N-terminal degradation of NLRP1 and CARD8 by the proteasome releases their C-terminal UPA-CARD fragments (CT) to form the inflammasome, which in turn activates caspase-1. Here, the authors present the cryo-EM structures of the NLRP1-CT and CARD8-CT helical filaments as well as the...

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Autores principales:	L. Robert Hollingsworth, Liron David, Yang Li, Andrew R. Griswold, Jianbin Ruan, Humayun Sharif, Pietro Fontana, Elizabeth L. Orth-He, Tian-Min Fu, Daniel A. Bachovchin, Hao Wu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0e61c5714aba4c07951365c347f3e523
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spelling	oai:doaj.org-article:0e61c5714aba4c07951365c347f3e5232021-12-02T11:46:01ZMechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes10.1038/s41467-020-20320-y2041-1723https://doaj.org/article/0e61c5714aba4c07951365c347f3e5232021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20320-yhttps://doaj.org/toc/2041-1723Pathogen triggered N-terminal degradation of NLRP1 and CARD8 by the proteasome releases their C-terminal UPA-CARD fragments (CT) to form the inflammasome, which in turn activates caspase-1. Here, the authors present the cryo-EM structures of the NLRP1-CT and CARD8-CT helical filaments as well as the ASC−caspase-1 octamer structure, which together with in vitro and cell based assays provide further insights into the architecture and specificity of the active NLRP1 and CARD8 inflammasomes.L. Robert HollingsworthLiron DavidYang LiAndrew R. GriswoldJianbin RuanHumayun SharifPietro FontanaElizabeth L. Orth-HeTian-Min FuDaniel A. BachovchinHao WuNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q L. Robert Hollingsworth Liron David Yang Li Andrew R. Griswold Jianbin Ruan Humayun Sharif Pietro Fontana Elizabeth L. Orth-He Tian-Min Fu Daniel A. Bachovchin Hao Wu Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
description	Pathogen triggered N-terminal degradation of NLRP1 and CARD8 by the proteasome releases their C-terminal UPA-CARD fragments (CT) to form the inflammasome, which in turn activates caspase-1. Here, the authors present the cryo-EM structures of the NLRP1-CT and CARD8-CT helical filaments as well as the ASC−caspase-1 octamer structure, which together with in vitro and cell based assays provide further insights into the architecture and specificity of the active NLRP1 and CARD8 inflammasomes.
format	article
author	L. Robert Hollingsworth Liron David Yang Li Andrew R. Griswold Jianbin Ruan Humayun Sharif Pietro Fontana Elizabeth L. Orth-He Tian-Min Fu Daniel A. Bachovchin Hao Wu
author_facet	L. Robert Hollingsworth Liron David Yang Li Andrew R. Griswold Jianbin Ruan Humayun Sharif Pietro Fontana Elizabeth L. Orth-He Tian-Min Fu Daniel A. Bachovchin Hao Wu
author_sort	L. Robert Hollingsworth
title	Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
title_short	Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
title_full	Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
title_fullStr	Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
title_full_unstemmed	Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
title_sort	mechanism of filament formation in upa-promoted card8 and nlrp1 inflammasomes
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/0e61c5714aba4c07951365c347f3e523
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Mechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes

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