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Monoubiquitination joins polyubiquitination as an esteemed proteasomal targeting signal
Author(s) -
Livneh Ido,
KravtsovaIvantsiv Yelena,
Braten Ori,
Kwon Yong Tae,
Ciechanover Aaron
Publication year - 2017
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201700027
Subject(s) - deubiquitinating enzyme , ubiquitin , proteasome , biology , ubiquitin conjugating enzyme , microbiology and biotechnology , protein degradation , ubiquitin ligase , biochemistry , gene
A polyubiquitin chain attached covalently to the target substrate has been recognized for long as the "canonical" proteasomal degradation signal. However, several proteins have been shown to be targeted for degradation following monoubiquitination, indicating that the proteasome can recognize signals other than a ubiquitin polymer. A comprehensive screen aiming at determining the extent of this mode of recognition revealed that ∼40% of mammalian and ∼20% of yeast proteins are degraded following monoubiquitination. Characterization of these proteins showed that on average, the monoubiquitinated proteins are smaller than the polyubiquitinated ones, and in humans, are less disordered. Further, proteins degraded by the two different modes belong to distinct functional groups. These findings along with detailed structural analysis of the proteasome, its ubiquitin receptors and deubiquitinating enzymes, suggest that the ubiquitin signal - its formation, recognition, editing, and removal - is far more complex and diverse than originally assumed. Also see the video abstract here: https://youtu.be/QKpN9c6Rg20.