Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10

Tal Keren-Kaplan, Ilan Attali, Olga Levin-Kravets, Oded Kleifeld, Shay Ben-Aroya, Gali Prag

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


Ubiquitylation is a posttranslational modification that determines protein fate. The ubiquitin code is written by enzymatic cascades of E1 and E2 and E3 enzymes. Ubiquitylation can be edited or erased by deubiquitylating enzymes. Ub-receptors are proteins that read and decipher the ubiquitin codes into cellular response. They harbor a ubiquitin-binding domain and a response element. Interestingly, Ub-receptors are also regulated by ubiquitylation and deubiquitylation. However, until recently, the molecular details and the significance of this regulation remained enigmatic. Rpn10 is a Ub-receptor that shuttles ubiquitylated targets to the proteasome for degradation. Here we review recent data on Rpn10, with emphasis on its regulation by ubiquitylation.
Original languageEnglish
Title of host publicationUbiquitin Proteasome System - Current Insights into Mechanism Cellular Regulation and Disease
EditorsMatthew Summers
ISBN (Electronic)9781838804916
StatePublished - 1 Jun 2019


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