| Online-Ressource |
Verfasst von: | Szórádi, Tamás [VerfasserIn]  |
| Schaeff, Katharina [VerfasserIn]  |
| Schmidt, Rolf [VerfasserIn]  |
| Bircham, Peter W. [VerfasserIn]  |
| Leiss, Kevin [VerfasserIn]  |
| Diaz-Miyar, Juan [VerfasserIn]  |
| Schuck, Sebastian [VerfasserIn]  |
Titel: | SHRED is a regulatory cascade that reprograms Ubr1 substrate specificity for enhanced protein quality control during stress |
Verf.angabe: | Tamas Szoradi, Katharina Schaeff, Enrique M. Garcia-Rivera, Daniel N. Itzhak, Rolf M. Schmidt, Peter W. Bircham, Kevin Leiss, Juan Diaz-Miyar, Vivian K. Chen, Dale Muzzey, Georg H. H. Borner, and Sebastian Schuck |
E-Jahr: | 2018 |
Jahr: | May 31, 2018 |
Umfang: | 19 S. |
Fussnoten: | Gesehen am 02.05.2019 |
Titel Quelle: | Enthalten in: Molecular cell |
Ort Quelle: | [Cambridge, Mass.] : Cell Press, 1997 |
Jahr Quelle: | 2018 |
Band/Heft Quelle: | 70(2018), 6, Seite 1025-1037, e1-e5 |
ISSN Quelle: | 1097-4164 |
Abstract: | Summary - When faced with proteotoxic stress, cells mount adaptive responses to eliminate aberrant proteins. Adaptive responses increase the expression of protein folding and degradation factors to enhance the cellular quality control machinery. However, it is unclear whether and how this augmented machinery acquires new activities during stress. Here, we uncover a regulatory cascade in budding yeast that consists of the hydrophilin protein Roq1/Yjl144w, the HtrA-type protease Ynm3/Nma111, and the ubiquitin ligase Ubr1. Various stresses stimulate ROQ1 transcription. The Roq1 protein is cleaved by Ynm3. Cleaved Roq1 interacts with Ubr1, transforming its substrate specificity. Altered substrate recognition by Ubr1 accelerates proteasomal degradation of misfolded as well as native proteins at the endoplasmic reticulum membrane and in the cytosol. We term this pathway stress-induced homeostatically regulated protein degradation (SHRED) and propose that it promotes physiological adaptation by reprogramming a key component of the quality control machinery. |
DOI: | doi:10.1016/j.molcel.2018.04.027 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.molcel.2018.04.027 |
| Volltext: http://www.sciencedirect.com/science/article/pii/S1097276518303496 |
| DOI: https://doi.org/10.1016/j.molcel.2018.04.027 |
Datenträger: | Online-Ressource |
Sprache: | eng |
Sach-SW: | protein degradation |
| protein misfolding |
| quality control |
| SHRED |
| stress |
| ubiquitin ligase |
K10plus-PPN: | 1664489401 |
Verknüpfungen: | → Zeitschrift |
SHRED is a regulatory cascade that reprograms Ubr1 substrate specificity for enhanced protein quality control during stress / Szórádi, Tamás [VerfasserIn]; May 31, 2018 (Online-Ressource)