Protein Synthesis and Degradation
The Human Selenoprotein VCP-interacting Membrane Protein (VIMP) Is Non-globular and Harbors a Reductase Function in an Intrinsically Disordered Region*

https://doi.org/10.1074/jbc.M112.346775Get rights and content
Under a Creative Commons license
open access

Background: Human VIMP/SelS is a selenoprotein involved in endoplasmic reticulum-associated degradation.

Results: The cytosolic domain of VIMP constitutes an extended α-helical segment followed by an intrinsically disordered region harboring redox activity.

Conclusion: VIMP is a non-globular protein with a likely reductase function.

Significance: These findings provide new mechanistic insight into the molecular function of VIMP.

Endoplasmic Reticulum Stress
Endoplasmic Reticulum(ER)
Protein Degradation
Protein Misfolding
Redox
Endoplasmic Reticulum-associated Degradation (ERAD)
Selenoprotein S (SelS)
VCP-interacting Membrane Protein (VIMP)
p97

Cited by (0)

Data deposition: Backbone chemical shifts have been deposited at the Biological Magnetic Resonance Bank with accession numbers: 18176 (oxidized cVIMP-Cys); 18177 (reduced cVIMP-Cys).

*

This work was funded by the Danish Council for Independent Research (Natural Sciences), Novo Nordisk Fonden, Lundbeckfonden, and the Alfred Benzon Foundation.

This article contains supplemental Fig. S1.

1

Recipient of a Novo Scholarship 2011.

2

Both authors contributed equally to this work.