Chapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10
Author(s)
Kleifeld, Oded
Levin-Kravets, Olga
Prag, Gali
Ben-Aroya, Shay
Attali, Ilan
Keren-Kaplan, Tal
Language
EnglishAbstract
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.
Keywords
ubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttleDOI
10.5772/intechopen.85283Publisher
InTechOpenPublisher website
https://www.intechopen.com/Publication date and place
2019Classification
Biochemistry