Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p.

@article{Williams2008Pex10pFA,
  title={Pex10p functions as an E3 ligase for the Ubc4p-dependent ubiquitination of Pex5p.},
  author={Chris Williams and M. van den Berg and E. Geers and B. Distel},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={374 4},
  pages={
          620-4
        }
}
  • Chris Williams, M. van den Berg, +1 author B. Distel
  • Published 2008
  • Biology, Medicine
  • Biochemical and biophysical research communications
  • The Saccharomyces cerevisiae (Sc) PTS1 import receptor Pex5p is modified by ubiquitin, both in an Ubc4p-dependent and a Pex4p (Ubc10p)-dependent manner. Both of these modifications require the RING domain-containing protein Pex10p in vivo, but the actual role this protein plays in the ubiquitination of Pex5p has so far, remained enigmatic. Here, we report that the RING domain of Pex10p exhibits E(3) ligase activity in vitro, in combination with the human E(2) enzyme UbcH5a, a homologue of… CONTINUE READING

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