Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2.

  title={Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2.},
  author={Mohamed Abu-Farha and Sylvain Lanouette and Fred Elisma and V{\'e}ronique Tremblay and Jeffery Butson and Daniel Figeys and Jean-François Couture},
  journal={Journal of molecular cell biology},
  volume={3 5},
The SMYD (SET and MYND domain) family of lysine methyltransferases (KMTs) plays pivotal roles in various cellular processes, including gene expression regulation and DNA damage response. Initially identified as genuine histone methyltransferases, specific members of this family have recently been shown to methylate non-histone proteins such as p53, VEGFR, and the retinoblastoma tumor suppressor (pRb). To gain further functional insights into this family of KMTs, we generated the protein… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS
26 Citations
63 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 26 extracted citations


Publications referenced by this paper.
Showing 1-10 of 63 references

Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase

  • M. A. Brown, R. J. Sims, III, Gottlieb, P.D
  • complex. Mol. Cancer
  • 2006
Highly Influential
8 Excerpts

Similar Papers

Loading similar papers…