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Ubiquitylated-Rpn10 - Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

ABSTRACT: MS/MS characterization of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state that together with structural and biochemical studies reveal a novel ubiquitin-binding patch on RPN10 that directs K84 ubiquitylation.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Oded Kleifeld

LAB HEAD: Gali Prag

PROVIDER: PXD004761 | Pride | 2018-10-26

REPOSITORIES: Pride

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Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.

Keren-Kaplan Tal T Zeev Peters Lee L Levin-Kravets Olga O Attali Ilan I Kleifeld Oded O Shohat Noa N Artzi Shay S Zucker Ori O Pilzer Inbar I Reis Noa N Glickman Michael H MH Ben-Aroya Shay S Prag Gali G

Nature communications 20161004

Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal ubiquitin-receptor Rpn10 in its ubiquitylated state. The structure shows a novel ubiquitin-binding patch that directs K84 ubiquitylation. Superimpositi ...[more]

PMID: 27698474

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