Journal
MOLECULAR CELL
Volume 63, Issue 6, Pages 1055-1065Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2016.08.005
Keywords
-
Categories
Funding
- bi-national USA-Israel Scientific Foundation [2011253]
- ISF I-CORE
- ERC [340712]
- European Research Council (ERC) [340712] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
The ubiquitin-proteasome system (UPS) for protein degradation has been under intensive study, and yet, we have only partial understanding of mechanisms by which proteins are selected to be targeted for proteolysis. One of the obstacles in studying these recognition pathways is the limited repertoire of known degradation signals (degrons). To better understand what determines the susceptibility of intracellular proteins to degradation by the UPS, we developed an unbiased method for large-scale identification of eukaryotic degrons. Using a reporter-based high-throughput competition assay, followed by deep sequencing, we measured a degradation potency index for thousands of native polypeptides in a single experiment. We further used this method to identify protein quality control (PQC)-specific and compartment-specific degrons. Our method provides an unprecedented insight into the yeast degronome, and it can readily be modified to study protein degradation signals and pathways in other organisms and in various settings.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available