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 α (TCR α) 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 α chain from the ER, as well as a truncated, mutant version of TCR α 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.
Original language | English |
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Pages (from-to) | 365-376 |
Number of pages | 12 |
Journal | Journal of Cell Biology |
Volume | 142 |
Issue number | 2 |
DOIs | |
State | Published - 27 Jul 1998 |
Externally published | Yes |
Keywords
- Class I heavy chain
- Degradation
- Diamide
- Human cytomegalovirus
- TCR α chain