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WDR5, a complexed protein

Nature Structural & Molecular Biology volume 16, pages 678–680 (2009)Cite this article

The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine–recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.

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Figure 1: Histone H3K4 methylation by yeast COMPASS and mammalian COMPASS-like complexes.
Figure 2: Structural basis for histone H3, MLL1 Win and WDR5 Ala12–Pro17 recognition by WDR5.

References

  1. Miller, T. et al. Proc. Natl. Acad. Sci. USA 98, 12902–12907 (2001).

    Article  CAS  Google Scholar 

  2. Roguev, A. et al. EMBO J. 20, 7137–7148 (2001).

    Article  CAS  Google Scholar 

  3. Shilatifard, A. Annu. Rev. Biochem. 75, 243–269 (2006).

    Article  CAS  Google Scholar 

  4. Krogan, N.J. et al. J. Biol. Chem. 277, 10753–10755 (2002).

    Article  CAS  Google Scholar 

  5. Steward, M.M. et al. Nat. Struct. Mol. Biol. 13, 852–854 (2006).

    Article  CAS  Google Scholar 

  6. Schneider, J. et al. Mol. Cell 19, 849–856 (2005).

    Article  CAS  Google Scholar 

  7. Schlichter, A. & Cairns, B.R. EMBO J. 24, 1222–1231 (2005).

    Article  CAS  Google Scholar 

  8. Morillon, A., Karabetsou, N., Nair, A. & Mellor, J. Mol. Cell 18, 723–734 (2005).

    Article  CAS  Google Scholar 

  9. Shilatifard, A. Curr. Opin. Cell Biol. 20, 341–348 (2008).

    Article  CAS  Google Scholar 

  10. Wysocka, J. et al. Cell 121, 859–872 (2005).

    Article  CAS  Google Scholar 

  11. Dou, Y. et al. Nat. Struct. Mol. Biol. 13, 713–719 (2006).

    Article  CAS  Google Scholar 

  12. Han, Z. et al. Mol. Cell 22, 137–144 (2006).

    Article  CAS  Google Scholar 

  13. Couture, J.F., Collazo, E. & Trievel, R.C. Nat. Struct. Mol. Biol. 13, 698–703 (2006).

    Article  CAS  Google Scholar 

  14. Ruthenburg, A.J. et al. Nat. Struct. Mol. Biol. 13, 704–712 (2006).

    Article  CAS  Google Scholar 

  15. Schuetz, A. et al. EMBO J. 25, 4245–4252 (2006).

    Article  CAS  Google Scholar 

  16. Southall, S.M., Wong, P.S., Odho, Z., Roe, S.M. & Wilson, J.R. Mol. Cell 33, 181–191 (2009).

    Article  CAS  Google Scholar 

  17. Patel, A., Vought, V.E., Dharmarajan, V. & Cosgrove, M.S. J. Biol. Chem. 283, 32162–32175 (2008).

    Article  CAS  Google Scholar 

  18. Patel, A., Dharmarajan, V. & Cosgrove, M.S. J. Biol. Chem. 283, 32158–32161 (2008).

    Article  CAS  Google Scholar 

  19. Song, J.J. & Kingston, R.E. J. Biol. Chem. 283, 35258–35264 (2008).

    Article  CAS  Google Scholar 

  20. Thompson, B.A., Tremblay, V., Lin, G. & Bochar, D.A. Mol. Cell. Biol. 28, 3894–3904 (2008).

    Article  CAS  Google Scholar 

  21. Suganuma, T. et al. Nat. Struct. Mol. Biol. 15, 364–372 (2008).

    Article  CAS  Google Scholar 

  22. Wang, Y.L., Faiola, F., Xu, M., Pan, S. & Martinez, E. J. Biol. Chem. 283, 33808–33815 (2008).

    Article  CAS  Google Scholar 

  23. Mendjan, S. et al. Mol. Cell 21, 811–823 (2006).

    Article  CAS  Google Scholar 

  24. Garapaty, S. et al. J. Biol. Chem. 12, 7542–7552 (2009).

    Article  Google Scholar 

Download references

Acknowledgements

We thank D. Bochar, J. Workman and E. Smith for reading the manuscript and providing insightful comments, and L. Shilatifard for editorial assistance. This work was supported by grants from the US National Institute of General Medical Sciences (NIGMS; 5R01GM073839) to R.C.T. and the US National Cancer Institute (NCI; 5R01CA089455) to A.S.H.

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Authors and Affiliations

  1. Raymond C. Trievel is in the Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.,

    Raymond C Trievel

  2. Ali Shilatifard is at The Stowers Institute for Medical Research, Kansas City, Missouri, USA. rtrievel@umich.edu; ash@stowers.org,

    Ali Shilatifard

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Trievel, R., Shilatifard, A. WDR5, a complexed protein. Nat Struct Mol Biol 16, 678–680 (2009). https://doi.org/10.1038/nsmb0709-678

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