A cytosolic redox enzyme in ER-associated degradation

The human selenoprotein VIMP interacts with several known components of the ERAD machinery, and has been proposed to recruit p97 to the ER membrane. VIMP contains a cytosolic domain of 141 residues, with the Sec residue located in the penultimate position. Using a combination of bioinformatics, fluorescence and CD spectroscopy, as well as NMR spectrometry we show that the protein contains an N-terminal α-helical region and a C-terminal disordered part. Our analysis also shows that the redox state of the protein influences local structural properties of the polypeptide chain in the C-terminal region. Finally, we present a characterization of in vitro redox properties of the protein.