IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal).

@article{Dunne2010IRAK1AI,
  title={IRAK1 and IRAK4 promote phosphorylation, ubiquitination, and degradation of MyD88 adaptor-like (Mal).},
  author={Aisling Dunne and Susan Carpenter and Constantinos Brikos and Pearl Gray and Astrid Strelow and Holger Wesche and Nick Morrice and Luke A J O'Neill},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 24},
  pages={18276-82}
}
Signal transduction by Toll-like receptor 2 (TLR2) and TLR4 requires the adaptors MyD88 and Mal (MyD88 adaptor-like) and serine/threonine kinases, interleukin-1 receptor-associated kinases IRAK1 and IRAK4. We have found that both IRAK1 and IRAK4 can directly phosphorylate Mal. In addition, co-expression of Mal with either IRAK resulted in depletion of Mal from cell lysates. This is likely to be due to Mal phosphorylation by the IRAKs because kinase-inactive forms of either IRAK had no effect… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

References

Publications referenced by this paper.

IRAK1 and IRAK4 Activity 18282 JOURNAL OF BIOLOGICAL CHEMISTRY

  • M. Kubo-Murai, K. Hazeki, K. Nigorikawa, T. Omoto, N. Inoue, O. Hazeki
  • J. Biochem. 143,
  • 2008

Similar Papers

Loading similar papers…