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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Terms

 

Gene Review: 

WDR5  -  WD repeat domain 5

Homo sapiens

Synonyms: BIG-3, BIG3, BMP2-induced 3-kb gene protein, CFAP89, SWD3, ...
 
 
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Disease relevance of WDR5

  • To identify a role for BIG-3 in osteoblast differentiation, MC3T3-E1 cells were stably transfected with the full-length coding region of BIG-3 (MC3T3E1-BIG-3) cloned downstream of a cytomegalovirus promoter in pcDNA3 [1].
 

High impact information on WDR5

  • A stable complex containing MLL1 and MOF has been immunoaffinity purified from a human cell line that stably expresses an epitope-tagged WDR5 subunit [2].
  • WDR5 is essential for vertebrate development, in that WDR5-depleted X. laevis tadpoles exhibit a variety of developmental defects and abnormal spatial Hox gene expression [3].
  • WDR5 is required for binding of the methyltransferase complex to the K4-dimethylated H3 tail as well as for global H3 K4 trimethylation and HOX gene activation in human cells [3].
  • Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5 [4].
  • Here, we show that CUL4-DDB1 complexes interact with multiple WD40-repeat proteins (WDRs) including TLE1-3, WDR5, L2DTL (also known as CDT2) and the Polycomb-group protein EED (also known as ESC) [5].
 

Biological context of WDR5

  • We propose a mechanism for the involvement of WDR5 in binding and presenting histone H3K4 for further methylation as a component of MLL complexes [6].
  • A common feature of several H3K4 methyltransferase complexes is the presence of three structural components (RbBP5, Ash2L and WDR5) and a catalytic subunit containing a SET domain [7].
  • WDR5 is a core component of SET1-family complexes that achieve transcriptional activation via methylation of histone H3 on Nzeta of Lys4 (H3K4) [8].
 

Anatomical context of WDR5

 

Associations of WDR5 with chemical compounds

  • The structures reveal that WDR5 is able to bind all of these histone H3 peptides, but only H3K4me2 peptide forms extra interactions with WDR5 by use of both water-mediated hydrogen bonding and the altered hydrophilicity of the modified lysine 4 [6].
  • Cyclic AMP production in response to parathyroid hormone was increased 10- and 14-fold at 7 and 14 days, respectively, in MC3T3E1-BIG-3 clones, relative to MC3T3E1-EV clones [1].
 

Other interactions of WDR5

References

  1. Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation. Gori, F., Divieti, P., Demay, M.B. J. Biol. Chem. (2001) [Pubmed]
  2. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Dou, Y., Milne, T.A., Tackett, A.J., Smith, E.R., Fukuda, A., Wysocka, J., Allis, C.D., Chait, B.T., Hess, J.L., Roeder, R.G. Cell (2005) [Pubmed]
  3. WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Wysocka, J., Swigut, T., Milne, T.A., Dou, Y., Zhang, X., Burlingame, A.L., Roeder, R.G., Brivanlou, A.H., Allis, C.D. Cell (2005) [Pubmed]
  4. Structural basis for the specific recognition of methylated histone H3 lysine 4 by the WD-40 protein WDR5. Han, Z., Guo, L., Wang, H., Shen, Y., Deng, X.W., Chai, J. Mol. Cell (2006) [Pubmed]
  5. CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation. Higa, L.A., Wu, M., Ye, T., Kobayashi, R., Sun, H., Zhang, H. Nat. Cell Biol. (2006) [Pubmed]
  6. Structural basis for molecular recognition and presentation of histone H3 By WDR5. Schuetz, A., Allali-Hassani, A., Martín, F., Loppnau, P., Vedadi, M., Bochkarev, A., Plotnikov, A.N., Arrowsmith, C.H., Min, J. EMBO J. (2006) [Pubmed]
  7. Regulation of MLL1 H3K4 methyltransferase activity by its core components. Dou, Y., Milne, T.A., Ruthenburg, A.J., Lee, S., Lee, J.W., Verdine, G.L., Allis, C.D., Roeder, R.G. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  8. Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex. Ruthenburg, A.J., Wang, W., Graybosch, D.M., Li, H., Allis, C.D., Patel, D.J., Verdine, G.L. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  9. Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes. Steward, M.M., Lee, J.S., O'donovan, A., Wyatt, M., Bernstein, B.E., Shilatifard, A. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  10. Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo. Gori, F., Friedman, L., Demay, M.B. Journal of musculoskeletal & neuronal interactions. (2005) [Pubmed]
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