Ubiquitin system: JAMMing in the name of the lid

Curr Biol. 2002 Dec 10;12(23):R815-7. doi: 10.1016/s0960-9822(02)01317-9.

Abstract

The isopeptide bonds formed by ubiquitin or its relatives are cleaved by hydrolases with active site cysteines. Recent studies have revealed that similar metalloprotease motifs--JAMMs--in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively.

Publication types

  • Review

MeSH terms

  • Metalloendopeptidases / metabolism*
  • Peptide Hydrolases / metabolism*
  • Proteasome Endopeptidase Complex*
  • Protein Subunits
  • Saccharomyces cerevisiae / enzymology
  • Signal Transduction
  • Ubiquitin / metabolism*

Substances

  • Protein Subunits
  • Ubiquitin
  • Peptide Hydrolases
  • Metalloendopeptidases
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease