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Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase

Selective protein degradation by the ubiquitin-proteasome system (UPS) is involved in all cellular processes. However, the substrates and specificity of most UPS components are not well understood. Here we systematically characterized the UPS in Saccharomyces cerevisiae. Using fluorescent timers, we...

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Main Authors: Kong, Ka-Yiu Edwin (Author) , Fischer, Bernd (Author) , Meurer, Matthias (Author) , Kats, Ilia (Author) , Liu, Zhaoyang (Author) , Rühle, Frank (Author) , Barry, Joseph D. (Author) , Kirrmaier, Daniel (Author) , Chevyreva, Veronika (Author) , San Luis, Bryan-Joseph (Author) , Costanzo, Michael (Author) , Huber, Wolfgang (Author) , Andrews, Brenda (Author) , Boone, Charles (Author) , Knop, Michael (Author) , Khmelinskii, Anton (Author)
Format: Article (Journal)
Language:English
Published: 3 June 2021
In: Molecular cell
Year: 2021, Volume: 81, Issue: 11, Pages: 2460-2476., e1-e11
ISSN:1097-4164
DOI:10.1016/j.molcel.2021.04.018
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.molcel.2021.04.018
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S1097276521003233
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Author Notes:Ka-Yiu Edwin Kong, Bernd Fischer, Matthias Meurer, Ilia Kats, Zhaoyan Li, Frank Rühle, Joseph D. Barry, Daniel Kirrmaier, Veronika Chevyreva, Bryan-Joseph San Luis, Michael Costanzo, Wolfgang Huber, Brenda J. Andrews, Charles Boone, Michael Knop, and Anton Khmelinskii
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Summary:Selective protein degradation by the ubiquitin-proteasome system (UPS) is involved in all cellular processes. However, the substrates and specificity of most UPS components are not well understood. Here we systematically characterized the UPS in Saccharomyces cerevisiae. Using fluorescent timers, we determined how loss of individual UPS components affects yeast proteome turnover, detecting phenotypes for 76% of E2, E3, and deubiquitinating enzymes. We exploit this dataset to gain insights into N-degron pathways, which target proteins carrying N-terminal degradation signals. We implicate Ubr1, an E3 of the Arg/N-degron pathway, in targeting mitochondrial proteins processed by the mitochondrial inner membrane protease. Moreover, we identify Ylr149c/Gid11 as a substrate receptor of the glucose-induced degradation-deficient (GID) complex, an E3 of the Pro/N-degron pathway. Our results suggest that Gid11 recognizes proteins with N-terminal threonines, expanding the specificity of the GID complex. This resource of potential substrates and relationships between UPS components enables exploring functions of selective protein degradation.
Item Description:Gesehen am 10.03.2022
Physical Description:Online Resource
ISSN:1097-4164
DOI:10.1016/j.molcel.2021.04.018

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