Numerous proteins with unique characteristics are degraded by the 26S proteasome following monoubiquitination.

ABSTRACT: The "canonical" proteasomal degradation signal is a substrate-anchored polyubiquitin chain. However, a handful of proteins were shown to be targeted following monoubiquitination. In this study, we established-in both human and yeast cells-a systematic approach for the identification of monoubiquitination-dependent proteasomal substrates. The cellular wild-type polymerizable ubiquitin was replaced with ubiquitin that cannot form chains. Using proteomic analysis, we screened for substrates that are nevertheless degraded under these conditions compared with those that are stabilized, and therefore require polyubiquitination for their degradation. For randomly sampled representative substrates, we confirmed that their cellular stability is in agreement with our screening prediction. Importantl

SUBMITTER: Braten O 

PROVIDER: S-EPMC4987823 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature