AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation

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 AMPylation and the burden of unfolded ER proteins sugge...

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Detalles Bibliográficos
Autores principales: Preissler, Steffen, Rohland, Lukas, Yan, Yahui, Chen, Ruming, Read, Randy J, Ron, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Biochemistry and Chemical Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5667935/
https://www.ncbi.nlm.nih.gov/pubmed/29064368
http://dx.doi.org/10.7554/eLife.29428

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5667935/
https://www.ncbi.nlm.nih.gov/pubmed/29064368
http://dx.doi.org/10.7554/eLife.29428

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