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STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif.

Conjugation with ubiquitin acts as a sorting signal for proteins in the endocytic and biosynthetic pathways at the endosome. Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown. Herein, we show that STAM proteins bind ubiquitin and ubiquitinated proteins and that the tandemly located VHS (Vps27/Hrs/STAM) domain and ubiquitin-interacting motif serve as the binding site(s). STAM proteins colocalize with Hrs on the early endosome. Overexpression of STAM proteins, but not their mutants lacking the ubiquitin-binding activity, causes the accumulation of ubiquitinated proteins and ligand-activated epidermal growth factor receptor on the early endosome. These results suggest that through interaction with ubiquitinated cargo proteins on the early endosome via the VHS domain and ubiquitin-interacting motif, STAM proteins participate in the sorting of cargo proteins for trafficking to the lysosome.

Pubmed ID: 12972556


  • Mizuno E
  • Kawahata K
  • Kato M
  • Kitamura N
  • Komada M


Molecular biology of the cell

Publication Data

September 15, 2003

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • COS Cells
  • Cercopithecus aethiops
  • Endocytosis
  • Endosomal Sorting Complexes Required for Transport
  • Endosomes
  • HeLa Cells
  • Humans
  • Phosphoproteins
  • Protein Structure, Tertiary
  • Protein Transport
  • Receptor, Epidermal Growth Factor
  • Ubiquitin