Unknown,Transcriptomics,Genomics,Proteomics

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Unfolded Protein Response


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. Set of arrays organized by shared biological context, such as organism, tumors types, processes, etc. Computed

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Max Diehn 

PROVIDER: E-GEOD-3130 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

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

Casagrande R R   Stern P P   Diehn M M   Shamu C C   Osario M M   Zúñiga M M   Brown P O PO   Ploegh H H  

Molecular cell 20000401 4


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.  ...[more]

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