Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Tal Keren-Kaplan, Lee Zeev Peters, Olga Levin-Kravets, Ilan Attali, Oded Kleifeld, Noa Shohat, Shay Artzi, Ori Zucker, Inbar Pilzer, Noa Reis, Michael H. Glickman, Shay Ben-Aroya and Gali Prag ()
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Tal Keren-Kaplan: George S. Wise Faculty of Life Sciences, Tel Aviv University
Lee Zeev Peters: Faculty of Life Sciences, Bar-Ilan University
Olga Levin-Kravets: George S. Wise Faculty of Life Sciences, Tel Aviv University
Ilan Attali: George S. Wise Faculty of Life Sciences, Tel Aviv University
Oded Kleifeld: Monash University
Noa Shohat: George S. Wise Faculty of Life Sciences, Tel Aviv University
Shay Artzi: George S. Wise Faculty of Life Sciences, Tel Aviv University
Ori Zucker: George S. Wise Faculty of Life Sciences, Tel Aviv University
Inbar Pilzer: George S. Wise Faculty of Life Sciences, Tel Aviv University
Noa Reis: Technion—Israel Institute of Technology
Michael H. Glickman: Technion—Israel Institute of Technology
Shay Ben-Aroya: Faculty of Life Sciences, Bar-Ilan University
Gali Prag: George S. Wise Faculty of Life Sciences, Tel Aviv University

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract 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. Superimposition of ubiquitylated-Rpn10 onto electron-microscopy models of proteasomes indicates that the Rpn10-conjugated ubiquitin clashes with Rpn9, suggesting that ubiquitylation might be involved in releasing Rpn10 from the proteasome. Indeed, ubiquitylation on immobilized proteasomes dissociates the modified Rpn10 from the complex, while unmodified Rpn10 mainly remains associated. In vivo experiments indicate that contrary to wild type, Rpn10-K84R is stably associated with the proteasomal subunit Rpn9. Similarly Rpn10, but not ubiquitylated-Rpn10, binds Rpn9 in vitro. Thus we suggest that ubiquitylation functions to dissociate modified ubiquitin receptors from their targets, a function that promotes cyclic activity of ubiquitin receptors.

Date: 2016
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DOI: 10.1038/ncomms12960

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