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Comment
. 2020 May;30(5):374-375.
doi: 10.1038/s41422-020-0306-9.

Proteasome phase separation: a novel layer of quality control

Victoria Cohen-Kaplan  1 , Ido Livneh  1 , Aaron Ciechanover  2
Affiliations
Comment

Proteasome phase separation: a novel layer of quality control

Victoria Cohen-Kaplan et al. Cell Res. 2020 May.
No abstract available

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Figures

Fig. 1
Fig. 1. Hyperosmotic stress induces polyubiquitination of faulty nuclear proteins along with RAD23B-mediated formation of proteolytic proteasome-containing foci.
a Cell under normal conditions. b Following hyperosmotic stress, ubiquitination of orphan, unassembled ribosomal proteins and other nuclear proteins is upregulated. c The ubiquitinated nuclear proteins are recognized by the UBA domain of RAD23B that induces the formation of Ub-chains/RAD23B phase-separated condensates. d RAD23B recruits the proteasome to the condensates via its UBL domain. e The proteasome and p97 degrade the ubiquitinated proteins.
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