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

Preissler, Steffen; Rohland, Lukas; Yan, Yahui; Chen, Ruming; Read, Randy J; Ron, David

Preissler, Steffen; Rohland, Lukas; Yan, Yahui; Chen, Ruming; Read, Randy J; Ron, David.

Affiliation

Preissler S; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Rohland L; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Yan Y; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Chen R; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Read RJ; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.
Ron D; Cambridge Institute for Medical Research, University of Cambridge, Cambridge, United Kingdom.

Elife ; 62017 10 24.

Article in En | MEDLINE | ID: mdl-29064368

Subject(s)

Adenosine Monophosphate/metabolism; Adenosine Triphosphatases/metabolism; Heat-Shock Proteins/metabolism; Protein Processing, Post-Translational; Adenosine Triphosphatases/chemistry; Adenosine Triphosphate/metabolism; Animals; Cricetinae; Crystallography, X-Ray; Endoplasmic Reticulum Chaperone BiP; Heat-Shock Proteins/chemistry; Hydrolysis; Models, Molecular; Protein Binding; Protein Conformation

Key words

AMPylation; BiP; Hsp70; J-proteins; biochemistry; biophysics; endoplasmic reticulum; none; structural biology

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Monophosphate / Protein Processing, Post-Translational / Adenosine Triphosphatases / Heat-Shock Proteins Type of study: Prognostic_studies Limits: Animals Language: En Journal: Elife Year: 2017 Type: Article Affiliation country: United kingdom

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