Lingering mysteries of ubiquitin-chain assembly

Cell. 2006 Jan 13;124(1):27-34. doi: 10.1016/j.cell.2005.12.025.

Abstract

The small protein ubiquitin is often linked to substrates as a polymer. Such polymers vary in both linkage and length, which has important consequences for their function. Surprisingly, the mechanisms of ubiquitin-chain assembly are still not known. Deciphering them will shed light on why substrates differ in the extent and timing of polyubiquitin modification and how ancillary ubiquitination factors function.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Binding Sites / physiology
  • Models, Molecular
  • Ubiquitin / biosynthesis*
  • Ubiquitin / chemistry
  • Ubiquitin / physiology
  • Ubiquitin-Protein Ligase Complexes / chemistry
  • Ubiquitin-Protein Ligase Complexes / physiology

Substances

  • Ubiquitin
  • Ubiquitin-Protein Ligase Complexes