Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12

Christiane Riedinger, Jonas Boehringer, Jean-Francois Trempe, Edward D Lowe, Nicholas R Brown, Kalle Gehring, Martin E M Noble, Colin Gordon, Jane A Endicott

Research output: Contribution to journalArticlepeer-review


Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 1:1 complex with Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.
Original languageEnglish
Pages (from-to)33992-4003
Number of pages12
JournalJournal of Biological Chemistry
Issue number44
Publication statusPublished - 29 Oct 2010


  • Calorimetry
  • Carrier Proteins
  • Humans
  • Kinetics
  • Lysine
  • Magnetic Resonance Spectroscopy
  • Polyubiquitin
  • Proteasome Endopeptidase Complex
  • Protein Binding
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Signal Transduction
  • Surface Plasmon Resonance
  • Ubiquitin
  • von Willebrand Factor


Dive into the research topics of 'Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12'. Together they form a unique fingerprint.

Cite this