Protein ubiquitination: CHIPping away the symmetry

Brenda A. Schulman, Zhijian J. Chen

Research output: Contribution to journalShort surveypeer-review

9 Scopus citations

Abstract

CHIP is a ubiquitin ligase implicated in the degradation of misfolded proteins. In the November 23 issue of Molecular Cell, Zhang et al. (2005) identified CHIP as a protein that interacts with the ubiquitin E2 complex Ubc13-Uev1A, which catalyzes the synthesis of Lys-63-linked polyubiquitin chains. Although the ubiquitin ligase activity of CHIP requires its dimerization through the U box domain, the crystal structure of the CHIP-E2 complex reveals that the protomers in the CHIP homodimer adopt distinct conformations such that only one U box of CHIP interacts with Ubc13.

Original languageEnglish (US)
Pages (from-to)653-655
Number of pages3
JournalMolecular cell
Volume20
Issue number5
DOIs
StatePublished - Dec 9 2005

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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