Investigating FICD mediated deAMPylation of BiP
The Hsp70 protein, BiP, is a major endoplasmic reticulum (ER) chaperone and is essential for maintaining protein folding homeostasis. The protein folding capacity of the ER is tightly linked to the amount and activity of BiP, through the unfolded protein response (UPR). This regulation is achieved at both a transcriptional and post-translational level, and deregulation is implicated in a number of disease states including type II diabetes. Covalent addition of an AMP moiety, onto Thr-518 of BiP, represents one such reversible post-translational modification. AMPylation inactivates BiP and, therefore, dynamically matches BiP activity to client protein load in the ER. The BiP AMPylation and deAMPylation reactions are both catalysed by the single active site of a bifunctional metazoan Fic protein, FICD. Mechanistic insight into the means of FICD-mediated eukaryotic deAMPylation is still lacking. Through analysis of selectively deuterated FICD/BiP complexes, by contrast variation SANS, we will be able determine the stoichiometry and internal arrangement of the deAMPylation complex. In so doing, we will further our understanding of eukaryotic deAMPylation and the post-translational UPR.
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Luke A Perera; MARTEL Anne; PREVOST Sylvain; RON David and ZACCAI Nathan. (2019). Investigating FICD mediated deAMPylation of BiP. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-963
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