Nature Communications (Oct 2016)

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,
  • Gali Prag

DOI
https://doi.org/10.1038/ncomms12960
Journal volume & issue
Vol. 7, no. 1
pp. 1 – 12

Abstract

Read online

Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissociation from the proteasome.