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  SHRED Is a Regulatory Cascade that Reprograms Ubr1 Substrate Specificity for Enhanced Protein Quality Control during Stress

Szoradi, T., Schaeff, K., Garcia-Rivera, E. M., Itzhak, D. N., Schmidt, R. M., Bircham, P. W., et al. (2018). SHRED Is a Regulatory Cascade that Reprograms Ubr1 Substrate Specificity for Enhanced Protein Quality Control during Stress. Molecular Cell, 70(6), 1025-1037.e5. doi:10.1016/j.molcel.2018.04.027.

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 Creators:
Szoradi, Tamas1, Author
Schaeff, Katharina1, Author
Garcia-Rivera, Enrique M.1, Author
Itzhak, Daniel N.2, Author              
Schmidt, Rolf M.1, Author
Bircham, Peter W.1, Author
Leiss, Kevin1, Author
Diaz-Miyar, Juan1, Author
Chen, Vivian K.1, Author
Muzzey, Dale1, Author
Borner, Georg H. H.3, Author              
Schuck, Sebastian1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3Borner, Georg / Systems Biology of Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_3060205              

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Free keywords: N-END RULE; YEAST SACCHAROMYCES-CEREVISIAE; TRANSMEMBRANE CONDUCTANCE REGULATOR; CYTOSOLIC MISFOLDED PROTEINS; SHOCK TRANSCRIPTION FACTOR; E3 UBIQUITIN LIGASES; ENDOPLASMIC-RETICULUM; FLUORESCENT PROTEIN; STRUCTURAL BASIS; DEGRADATIONBiochemistry & Molecular Biology; Cell Biology;
 Abstract: 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.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 70 (6) Sequence Number: - Start / End Page: 1025 - 1037.e5 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929