A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems

Trends Biochem Sci. 2001 Jun;26(6):347-50. doi: 10.1016/s0968-0004(01)01835-7.


Ubiquitination generally serves as a signal for targeting cytoplasmic and nuclear proteins to the proteasome for subsequent degradation. Recently, evidence has accumulated indicating that ubiquitination also plays an important role in targeting integral membrane proteins for degradation by the lytic vacuole or the lysosome. This article describes a conserved protein motif, based on a sequence of the proteasomal component Rpn10/S5a, that is known to recognize ubiquitin. The presence of this motif in Eps15, Epsin and HRS, proteins involved in ligand-activated receptor endocytosis and degradation, suggest a more general role in ubiquitin recognition.

MeSH terms

  • Amino Acid Motifs*
  • Amino Acid Sequence
  • Animals
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism*
  • Humans
  • Hydrolysis
  • Lysosomes / metabolism*
  • Molecular Sequence Data
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • Proteasome Endopeptidase Complex
  • Proteins / chemistry
  • Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Ubiquitins / metabolism*


  • Multienzyme Complexes
  • Proteins
  • Ubiquitins
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex