Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential

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Item Type:	Article
Title:	Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential
Creators Name:	Tortorella, D., Story, C.M., Huppa, J.B., Wiertz, E.J., Jones, T.R. and Ploegh, H.L.
Abstract:	The human cytomegalovirus (HCMV) gene products US2 and US11 dislocate major histocompatibility class I heavy chains from the ER and target them for proteasomal degradation in the cytosol. The dislocation reaction is inhibited by agents that affect intracellular redox potential and/or free thiol status, such as diamide and N-ethylmaleimide. Subcellular fractionation experiments indicate that this inhibition occurs at the stage of discharge from the ER into the cytosol. The T cell receptor alpha (TCR alpha) chain is also degraded by a similar set of reactions, yet in a manner independent of virally encoded gene products. Diamide and N-ethylmaleimide likewise inhibit the dislocation of the full-length TCR alpha chain from the ER, as well as a truncated, mutant version of TCR alpha chain that lacks cysteine residues. Cytosolic destruction of glycosylated, ER-resident type I membrane proteins, therefore, requires maintenance of a proper redox potential for the initial step of removal of the substrate from the ER environment.
Keywords:	Diamide, Class I Heavy Chain, Degradation, Human Cytomegalovirus, TCR a Chain
Source:	Journal of Cell Biology
ISSN:	0021-9525
Publisher:	Rockefeller University Press
Volume:	142
Number:	2
Page Range:	365-76
Date:	27 July 1998
Official Publication:	https://doi.org/10.1083/jcb.142.2.365
PubMed:	View item in PubMed

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