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. 2000 Apr;5(4):729-35.
doi: 10.1016/s1097-2765(00)80251-8.

Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway

R Casagrande  1 , P Stern, M Diehn, C Shamu, M Osario, M Zúñiga, P O Brown, H Ploegh
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Free article

Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway

R Casagrande et al. Mol Cell. 2000 Apr.
Free article

Abstract

To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a proteasome-dependent manner. The overexpression of H-2K(b) heavy chains induces the unfolded protein response (UPR). In yeast mutants unable to mount the UPR, H-2K(b) heavy chains are greatly stabilized. This defect in degradation is suppressed by the expression of the active form of Hac1p, the transcription factor that upregulates UPR-induced genes. These results indicate that induction of the UPR is required for the degradation of protein substrates from the ER.

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