The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains

@article{Marteijn2009TheUL,
  title={The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains},
  author={Jurgen A Marteijn and Laurens T. van der Meer and Judith J. Smit and Sylvie M Noordermeer and Willemijn M Wissink and Patty Micha{\"e}la Jansen and Herman G. P. Swarts and Richard Hibbert and T. J. M. de Witte and Titia Sixma and Joop H Jansen and B A van der Reijden},
  journal={Leukemia},
  year={2009},
  volume={23},
  pages={1480-1489}
}
Ubiquitination plays a major role in many aspects of hematopoiesis. Alterations in ubiquitination have been implicated in hematological cancer. The ubiquitin ligase Triad1 controls the proliferation of myeloid cells. Here, we show that two RING (really interesting new gene) domains in Triad1 differentially bind ubiquitin-conjugating enzymes, UbcH7 and Ubc13. UbcH7 and Ubc13 are known to catalyze the formation of different poly-ubiquitin chains. These chains mark proteins for proteasomal… CONTINUE READING

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