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dc.contributor.authorKleifeld, Oded
dc.contributor.authorLevin-Kravets, Olga
dc.contributor.authorPrag, Gali
dc.contributor.authorBen-Aroya, Shay
dc.contributor.authorAttali, Ilan
dc.contributor.authorKeren-Kaplan, Tal
dc.date.accessioned2021-06-02T10:12:24Z
dc.date.available2021-06-02T10:12:24Z
dc.date.issued2019
dc.identifierONIX_20210602_10.5772/intechopen.85283_448
dc.identifier.urihttps://library.oapen.org/handle/20.500.12657/49334
dc.description.abstractUbiquitylation 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.
dc.languageEnglish
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistryen_US
dc.subject.otherubiquitin receptor, crystal structure, ubiquitylated ubiquitin receptor, regulation mechanisms, cargo shuttle
dc.titleChapter Structural Insight into Regulation of the Proteasome Ub-Receptor Rpn10
dc.typechapter
oapen.identifier.doi10.5772/intechopen.85283
oapen.relation.isPublishedBy09f6769d-48ed-467d-b150-4cf2680656a1
oapen.relation.isFundedByFP7-PEOPLE-IRG-2008
oapen.grant.number231079
oapen.grant.acronymAUTO-UBIQUITYLATION


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