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Autor:
Luke A. Perera, Steffen Preissler, Nathan R. Zaccai, Sylvain Prévost, Juliette M. Devos, Michael Haertlein, David Ron
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
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 mechan
Externí odkaz:
https://doaj.org/article/b1546d211ae74008933f9a4fd1200d65
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
The role of mesencephalic astrocyte-derived neurotrophic factor (MANF) in maintenance of protein folding homeostasis inside the ER has remained unclear. Here the authors determine the structure of the complex between MANF and the ER-localized chapero
Externí odkaz:
https://doaj.org/article/29a9184db10c451b966d07b035dde1b3
Publikováno v:
eLife, Vol 9 (2020)
The metazoan endoplasmic reticulum (ER) serves both as a hub for maturation of secreted proteins and as an intracellular calcium storage compartment, facilitating calcium-release-dependent cellular processes. ER calcium depletion robustly activates t
Externí odkaz:
https://doaj.org/article/2df68a40864044a2966b41fdb69dcf50
Publikováno v:
eLife, Vol 6 (2017)
The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client proteins in a process that is tightly coupled to ATP binding and hydrolysis. The inverse correlation between BiP AMPyl
Externí odkaz:
https://doaj.org/article/dea71c6fa26646bfb0446cd3cef77811
Autor:
Steffen Preissler, Cláudia Rato, Ruming Chen, Robin Antrobus, Shujing Ding, Ian M Fearnley, David Ron
Publikováno v:
eLife, Vol 4 (2015)
The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP affects protein folding homeostasis and the response to ER stress. Reversible inactivating covalent modification of BiP is believed to contribute to the balance between chaperones and unfol
Externí odkaz:
https://doaj.org/article/6ab11f0653ec45bd9fb9b9d3b257f33e
Autor:
Steffen Preissler, Joseph E Chambers, Ana Crespillo-Casado, Edward Avezov, Elena Miranda, Juan Perez, Linda M Hendershot, Heather P Harding, David Ron
Publikováno v:
eLife, Vol 4 (2015)
DnaK/Hsp70 chaperones form oligomers of poorly understood structure and functional significance. Site-specific proteolysis and crosslinking were used to probe the architecture of oligomers formed by the endoplasmic reticulum (ER) Hsp70, BiP. These we
Externí odkaz:
https://doaj.org/article/645adf268a244bb8b406109511db4a8a