Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD

The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient FICD:BiP complex and determine its crystal struct...

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Autores principales:	Joel Fauser, Burak Gulen, Vivian Pogenberg, Christian Pett, Danial Pourjafar-Dehkordi, Christoph Krisp, Dorothea Höpfner, Gesa König, Hartmut Schlüter, Matthias J. Feige, Martin Zacharias, Christian Hedberg, Aymelt Itzen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5b881075f8d343709870eb7b338a3da3
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spelling	oai:doaj.org-article:5b881075f8d343709870eb7b338a3da32021-12-02T17:33:33ZSpecificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD10.1038/s41467-021-22596-02041-1723https://doaj.org/article/5b881075f8d343709870eb7b338a3da32021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22596-0https://doaj.org/toc/2041-1723The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient FICD:BiP complex and determine its crystal structure.Joel FauserBurak GulenVivian PogenbergChristian PettDanial Pourjafar-DehkordiChristoph KrispDorothea HöpfnerGesa KönigHartmut SchlüterMatthias J. FeigeMartin ZachariasChristian HedbergAymelt ItzenNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joel Fauser Burak Gulen Vivian Pogenberg Christian Pett Danial Pourjafar-Dehkordi Christoph Krisp Dorothea Höpfner Gesa König Hartmut Schlüter Matthias J. Feige Martin Zacharias Christian Hedberg Aymelt Itzen Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
description	The ER chaperone BiP is critical for the unfolded protein response and tightly regulated through reversible AMPylation by FICD, but the structural basis is unknown. Here the authors use thiol-reactive nucleotide derivatives to stabilize the transient FICD:BiP complex and determine its crystal structure.
format	article
author	Joel Fauser Burak Gulen Vivian Pogenberg Christian Pett Danial Pourjafar-Dehkordi Christoph Krisp Dorothea Höpfner Gesa König Hartmut Schlüter Matthias J. Feige Martin Zacharias Christian Hedberg Aymelt Itzen
author_facet	Joel Fauser Burak Gulen Vivian Pogenberg Christian Pett Danial Pourjafar-Dehkordi Christoph Krisp Dorothea Höpfner Gesa König Hartmut Schlüter Matthias J. Feige Martin Zacharias Christian Hedberg Aymelt Itzen
author_sort	Joel Fauser
title	Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
title_short	Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
title_full	Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
title_fullStr	Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
title_full_unstemmed	Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
title_sort	specificity of ampylation of the human chaperone bip is mediated by tpr motifs of ficd
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5b881075f8d343709870eb7b338a3da3
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Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD

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