Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD

The ER chaperone BiP is regulated by FICD-mediated AMPylation and deAMPylation. Here, the authors characterise the structure of mammalian AMPylated BiP bound to FICD, by X-ray crystallography and neutron scattering, providing insights into the mechanism of BiP AMPylation and deAMPylation.

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Autores principales:	Luke A. Perera, Steffen Preissler, Nathan R. Zaccai, Sylvain Prévost, Juliette M. Devos, Michael Haertlein, David Ron
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b1546d211ae74008933f9a4fd1200d65
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spelling	oai:doaj.org-article:b1546d211ae74008933f9a4fd1200d652021-12-02T17:08:38ZStructures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD10.1038/s41467-021-25076-72041-1723https://doaj.org/article/b1546d211ae74008933f9a4fd1200d652021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25076-7https://doaj.org/toc/2041-1723The ER chaperone BiP is regulated by FICD-mediated AMPylation and deAMPylation. Here, the authors characterise the structure of mammalian AMPylated BiP bound to FICD, by X-ray crystallography and neutron scattering, providing insights into the mechanism of BiP AMPylation and deAMPylation.Luke A. PereraSteffen PreisslerNathan R. ZaccaiSylvain PrévostJuliette M. DevosMichael HaertleinDavid RonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Luke A. Perera Steffen Preissler Nathan R. Zaccai Sylvain Prévost Juliette M. Devos Michael Haertlein David Ron Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
description	The ER chaperone BiP is regulated by FICD-mediated AMPylation and deAMPylation. Here, the authors characterise the structure of mammalian AMPylated BiP bound to FICD, by X-ray crystallography and neutron scattering, providing insights into the mechanism of BiP AMPylation and deAMPylation.
format	article
author	Luke A. Perera Steffen Preissler Nathan R. Zaccai Sylvain Prévost Juliette M. Devos Michael Haertlein David Ron
author_facet	Luke A. Perera Steffen Preissler Nathan R. Zaccai Sylvain Prévost Juliette M. Devos Michael Haertlein David Ron
author_sort	Luke A. Perera
title	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
title_short	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
title_full	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
title_fullStr	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
title_full_unstemmed	Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
title_sort	structures of a deampylation complex rationalise the switch between antagonistic catalytic activities of ficd
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b1546d211ae74008933f9a4fd1200d65
work_keys_str_mv	AT lukeaperera structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT steffenpreissler structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT nathanrzaccai structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT sylvainprevost structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT juliettemdevos structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT michaelhaertlein structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd AT davidron structuresofadeampylationcomplexrationalisetheswitchbetweenantagonisticcatalyticactivitiesofficd
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Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD

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