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Gene Review

Wdr1  -  WD repeat domain 1

Mus musculus

Synonyms: AIP1, Actin-interacting protein 1, Aip1, D5Wsu185e, WD repeat-containing protein 1, ...
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Disease relevance of Wdr1


High impact information on Wdr1

  • We have identified a WD repeat host protein that was recruited to and actively retained on phagosomes by living, but not dead, mycobacteria [3].
  • In humans, this disease is caused by mutations in the AAAS gene, which encodes ALADIN, a protein that belongs to the family of WD-repeat proteins and localizes to nuclear pore complexes [4].
  • The WD repeat scaffolding protein RACK1 can mediate integration of the insulin-like growth factor I receptor (IGF-IR) and integrin signaling in transformed cells [5].
  • One conserved PcG complex, PRC2, is composed of several proteins including the histone methyltransferase (HMTase) Ezh2, the WD-repeat protein Eed, and the Zn-finger protein Suz12 [6].
  • Coronins are a conserved family of WD repeat-containing, actin-binding proteins that regulate cell motility in a variety of model organisms [7].

Biological context of Wdr1

  • This could lead to permanent overexpresssion of the ect-2, calnexin, and Wdr1 genes and suppression of expression of the DRIP/TRAP-80 gene that we observed, which likely contribute to induction and maintenance of transformed phenotypes [8].
  • Expression of the calnexin gene (encoding a type I membrane protein/molecular chaperone), the ect-2 proto-oncogene, and the stress-inducible gene, Wdr1, was upregulated [9].
  • Deletion of the C-terminal 41 residues of HEED, spanning the seventh WD repeat, as in the 494-residue HEED protein, was detrimental to HEED-MA interaction in vivo, suggesting the existence of another C-terminal binding site and/or a conformational role of the HEED C-terminal domain in the MA-HEED interaction [10].
  • To the best of our knowledge, this is the first report of tyrosine phosphorylation of a member of the WD repeat family of proteins [11].
  • Alix/AIP1 is a cytoplasmic protein, which was first characterized as an interactor of ALG-2, a calcium-binding protein necessary for cell death [12].

Anatomical context of Wdr1

  • In contrast, neither the coiled coil nor the positively charged residues within the linker domain were required for plasma membrane binding, suggesting that the N-terminal, WD repeat-containing domain mediates membrane interaction [13].
  • Association with the cytoskeleton was mediated by trimerization of a stretch of positively charged residues within a linker region between the N-terminal, WD repeat-containing domain and the C-terminal coiled coil [13].
  • The WD-repeat protein family consists of a large group of structurally related yet functionally diverse proteins found predominantly in eukaryotic cells [14].
  • Isolation and characterization of human and mouse WDR19,a novel WD-repeat protein exhibiting androgen-regulated expression in prostate epithelium [15].

Associations of Wdr1 with chemical compounds


Other interactions of Wdr1

  • Fragment R3-2 was a sequence in the mouse calnexin gene, fragment R3-1 a portion of the Wdr1 gene, and fragment R2-4 a portion of the ect-2 protooncogene [8].
  • Wdr12, a mouse gene encoding a novel WD-Repeat Protein with a notchless-like amino-terminal domain [14].
  • BACKGROUND: The retinoblastoma (Rb) suppressor-associated protein 46 (RbAp46) is a member of the WD-repeat protein family and a component of histone modifying and remodeling complexes [18].


  1. Structural organization and developmental expression pattern of the mouse WD-repeat gene DMR-N9 immediately upstream of the myotonic dystrophy locus. Jansen, G., Bächner, D., Coerwinkel, M., Wormskamp, N., Hameister, H., Wieringa, B. Hum. Mol. Genet. (1995) [Pubmed]
  2. Characterisation and expression analysis of the WDR9 gene, located in the Down critical region-2 of the human chromosome 21. Ramos, V.C., Vidal-Taboada, J., Bergoñon, S., Egeo, A., Fisher, E.M., Scartezzini, P., Oliva, R. Biochim. Biophys. Acta (2002) [Pubmed]
  3. A coat protein on phagosomes involved in the intracellular survival of mycobacteria. Ferrari, G., Langen, H., Naito, M., Pieters, J. Cell (1999) [Pubmed]
  4. Mice lacking the nuclear pore complex protein ALADIN show female infertility but fail to develop a phenotype resembling human triple A syndrome. Huebner, A., Mann, P., Rohde, E., Kaindl, A.M., Witt, M., Verkade, P., Jakubiczka, S., Menschikowski, M., Stoltenburg-Didinger, G., Koehler, K. Mol. Cell. Biol. (2006) [Pubmed]
  5. Insulin-like growth factor I controls a mutually exclusive association of RACK1 with protein phosphatase 2A and beta1 integrin to promote cell migration. Kiely, P.A., O'Gorman, D., Luong, K., Ron, D., O'Connor, R. Mol. Cell. Biol. (2006) [Pubmed]
  6. The murine polycomb group protein Eed is required for global histone H3 lysine-27 methylation. Montgomery, N.D., Yee, D., Chen, A., Kalantry, S., Chamberlain, S.J., Otte, A.P., Magnuson, T. Curr. Biol. (2005) [Pubmed]
  7. Phosphorylation of coronin 1B by protein kinase C regulates interaction with Arp2/3 and cell motility. Cai, L., Holoweckyj, N., Schaller, M.D., Bear, J.E. J. Biol. Chem. (2005) [Pubmed]
  8. Molecular biology of deregulated gene expression in transformed C3H/10T1/2 mouse embryo cell lines induced by specific insoluble carcinogenic nickel compounds. Landolph, J.R., Verma, A., Ramnath, J., Clemens, F. Environ. Health Perspect. (2002) [Pubmed]
  9. Molecular biology of nickel carcinogenesis: identification of differentially expressed genes in morphologically transformed C3H10T1/2 Cl 8 mouse embryo fibroblast cell lines induced by specific insoluble nickel compounds. Verma, R., Ramnath, J., Clemens, F., Kaspin, L.C., Landolph, J.R. Mol. Cell. Biochem. (2004) [Pubmed]
  10. HEED, the product of the human homolog of the murine eed gene, binds to the matrix protein of HIV-1. Peytavi, R., Hong, S.S., Gay, B., d'Angeac, A.D., Selig, L., Bénichou, S., Benarous, R., Boulanger, P. J. Biol. Chem. (1999) [Pubmed]
  11. The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. Chang, B.Y., Chiang, M., Cartwright, C.A. J. Biol. Chem. (2001) [Pubmed]
  12. Alix, a protein regulating endosomal trafficking, is involved in neuronal death. Trioulier, Y., Torch, S., Blot, B., Cristina, N., Chatellard-Causse, C., Verna, J.M., Sadoul, R. J. Biol. Chem. (2004) [Pubmed]
  13. Association of the leukocyte plasma membrane with the actin cytoskeleton through coiled coil-mediated trimeric coronin 1 molecules. Gatfield, J., Albrecht, I., Zanolari, B., Steinmetz, M.O., Pieters, J. Mol. Biol. Cell (2005) [Pubmed]
  14. Wdr12, a mouse gene encoding a novel WD-Repeat Protein with a notchless-like amino-terminal domain. Nal, B., Mohr, E., Silva, M.I., Tagett, R., Navarro, C., Carroll, P., Depetris, D., Verthuy, C., Jordan, B.R., Ferrier, P. Genomics (2002) [Pubmed]
  15. Isolation and characterization of human and mouse WDR19,a novel WD-repeat protein exhibiting androgen-regulated expression in prostate epithelium. Lin, B., White, J.T., Utleg, A.G., Wang, S., Ferguson, C., True, L.D., Vessella, R., Hood, L., Nelson, P.S. Genomics (2003) [Pubmed]
  16. The polysaccharide fraction AIP1 from Artemisia iwayomogi suppresses apoptotic death of the mouse spleen cells in culture. Hwang, J.S., Chung, H.K., Bae, E.K., Lee, A.Y., Ji, H.J., Park, D.W., Jung, H.J., Cho, C.W., Choi, H.J., Lee, D.S., Lee, K.R., Youn, H.J. Arch. Pharm. Res. (2003) [Pubmed]
  17. A carbohydrate fraction, AIP1, from Artemisia iwayomogi down-regulates Fas gene expression and suppresses apoptotic death of the thymocytes induced by 2,3,7,8-tectrachlorodibenzo-p-dioxin. Ji, H.J., Yeo, H.K., Lee, N.H., Hwang, J.S., Koo, K.A., Cheong, S.W., Park, J.H., Oh, G.S., Yoon, C.S., Youn, H.J. Biotechnol. Lett. (2005) [Pubmed]
  18. Inducible expression of RbAp46 activates c-Jun NH2-terminal kinase-dependent apoptosis and suppresses progressive growth of tumor xenografts in nude mice. Zhang, T.F., Yu, S.Q., Loggie, B.W., Wang, Z.Y. Anticancer Res. (2003) [Pubmed]
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