Protein ubiquitination

CHIPping away the symmetry

Brenda A. Schulman, Zhijian J. Chen

Research output: Contribution to journalArticle

9 Citations (Scopus)

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)653-659
Number of pages7
JournalMolecular Cell
Volume20
Issue number5
DOIs
StatePublished - Dec 9 2005

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Ubiquitination
Ubiquitin
Ligases
Polyubiquitin
Proteins
Protein Subunits
Dimerization
Proteolysis

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Protein ubiquitination : CHIPping away the symmetry. / Schulman, Brenda A.; Chen, Zhijian J.

In: Molecular Cell, Vol. 20, No. 5, 09.12.2005, p. 653-659.

Research output: Contribution to journalArticle

Schulman, Brenda A. ; Chen, Zhijian J. / Protein ubiquitination : CHIPping away the symmetry. In: Molecular Cell. 2005 ; Vol. 20, No. 5. pp. 653-659.
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