The Unfolded Protein Response Triggers Selective mRNA Release from the Endoplasmic Reticulum
| Autor: | Qiang Chen, Christopher V. Nicchitta, David W. Reid, Angeline S.-L. Tay, Shirish Shenolikar |
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| Jazyk: | angličtina |
| Předmět: |
Biology
Endoplasmic Reticulum Article General Biochemistry Genetics and Molecular Biology Mice Open Reading Frames Cytosol Polysome Gene expression Protein biosynthesis Animals RNA Messenger Biochemistry Genetics and Molecular Biology(all) Endoplasmic reticulum Translation (biology) Fibroblasts Cell biology Dithiothreitol Kinetics Proteostasis Biochemistry Polyribosomes Protein Biosynthesis Unfolded Protein Response Unfolded protein response Protein folding |
| Zdroj: | Cell. (6):1362-1374 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/j.cell.2014.08.012 |
| Popis: | SummaryThe unfolded protein response (UPR) is a stress response program that reprograms cellular translation and gene expression in response to proteotoxic stress in the endoplasmic reticulum (ER). One of the primary means by which the UPR alleviates this stress is by reducing protein flux into the ER via a general suppression of protein synthesis and ER-specific mRNA degradation. We report here an additional UPR-induced mechanism for the reduction of protein flux into the ER, where mRNAs that encode signal sequences are released from the ER to the cytosol. By removing mRNAs from the site of translocation, this mechanism may serve as a potent means to transiently reduce ER protein folding load and restore proteostasis. These findings identify the dynamic subcellular localization of mRNAs and translation as a selective and rapid regulatory feature of the cellular response to protein folding stress. |
| Databáze: | OpenAIRE |
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