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Gene Review

FOXG1  -  forkhead box G1

Homo sapiens

 
 
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Disease relevance of FOXG1B

 

Psychiatry related information on FOXG1B

 

High impact information on FOXG1B

  • This analysis revealed that the human QIN gene maps to chromosome region 14q11.2-->14q32, between the TCR and IGH loci [6].
  • Chromosomal mapping of the human QIN gene (renamed FKH2 by the Human Genome Organization Nomenclature Committee) was initially accomplished by correlation of the presence of the QIN locus with specific chromosome regions in a rodent-human hybrid panel [6].
  • DNA-binding protein blotting, UV crosslinking, and electroelution experiments were used to characterize the two hMREa-binding factors, termed BF1 and BF2 [7].
  • It is shown here that BF-1 interacts in vivo with global transcriptional corepressors of the Groucho family and also associates with the histone deacetylase 1 protein [8].
  • Taken together with the demonstration that these proteins are coexpressed in telencephalic neural progenitor cells, these results also suggest that complexes of BF-1, Groucho, and Hes factors may be involved in the regulation of progenitor cell differentiation in the telencephalon [8].
 

Biological context of FOXG1B

 

Anatomical context of FOXG1B

  • Some unusual T-cell phenotypes, with respect to the pattern of expression of BF1 antigen and CD3, were observed [1].
  • BF1 was superior to the other two antibodies, especially for lymphoid cells in cytospin preparations [1].
  • These antibodies were all satisfactory in the staining of normal peripheral lymphoid tissues and cortical thymic lymphocytes were reactive with BF1 and BF2 but not with WT31 [1].
 

Associations of FOXG1B with chemical compounds

  • When this metronidazole time course was simulated in vitro, the time to 99.9% kill ranged from 1.0 to 1.4 h for BF125 and from 1.8 to 3.5 h for BF1, while the eradication time ranged from 1.7 to 2.5 h and from 3.4 to 6.5 h, respectively [13].
 

Physical interactions of FOXG1B

  • At the genomic level the gene for HBF-1 contains an 500 bp intron situated between the DNA binding domain II and the fork head domain while that of HBF-2 is intronless [9].
 

Other interactions of FOXG1B

  • Because both BF-1 and PAX proteins interact with members of the groucho co-repressor family, it is plausible that PLU-1 has a role in groucho-mediated transcriptional repression [14].
  • HFK2 and HFK3 were found to be closely related but different from HFK1 [15].
  • Repression of CDC28 reduces the expression of the morphology-related transcription factors, Efg1p, Nrg1p, Rbf1p, Rim101p, Fkh2p and Tec1p and induces cell elongation in Candida albicans [16].
 

Analytical, diagnostic and therapeutic context of FOXG1B

References

  1. T-cell receptor antibodies in the immunohistochemical studies of normal and malignant lymphoid cells. Chan, W.C., Borowitz, M.J., Hammami, A., Wu, Y.J., Ip, S.J. Cancer (1988) [Pubmed]
  2. Transcription factor PRDII-BF1 activates human immunodeficiency virus type 1 gene expression. Seeler, J.S., Muchardt, C., Suessle, A., Gaynor, R.B. J. Virol. (1994) [Pubmed]
  3. Phylogenetic analysis of Brazilian HIV type 1 subtype D strains: tracing the origin of this subtype in Brazil. Couto-Fernandez, J.C., Eyer-Silva, W.A., Guimarães, M.L., Chequer-Fernandez, S.L., Grinsztejn, B., Delaporte, E., Peeters, M., Morgado, M.G. AIDS Res. Hum. Retroviruses (2006) [Pubmed]
  4. Definitive identification of human T cells in formalin fixed paraffin wax embedded tissue. Francis, N.D., Clark, D.M., Boylston, A.W. J. Clin. Pathol. (1988) [Pubmed]
  5. Haploinsufficiency of novel FOXG1B variants in a patient with severe mental retardation, brain malformations and microcephaly. Shoichet, S.A., Kunde, S.A., Viertel, P., Schell-Apacik, C., von Voss, H., Tommerup, N., Ropers, H.H., Kalscheuer, V.M. Hum. Genet. (2005) [Pubmed]
  6. The human homologue of the retroviral oncogene qin maps to chromosome 14q13. Kastury, K., Li, J., Druck, T., Su, H., Vogt, P.K., Croce, C.M., Huebner, K. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  7. Zinc rapidly induces a metal response element-binding factor. Czupryn, M., Brown, W.E., Vallee, B.L. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. The winged-helix protein brain factor 1 interacts with groucho and hes proteins to repress transcription. Yao, J., Lai, E., Stifani, S. Mol. Cell. Biol. (2001) [Pubmed]
  9. The genes for human brain factor 1 and 2, members of the fork head gene family, are clustered on chromosome 14q. Wiese, S., Murphy, D.B., Schlung, A., Burfeind, P., Schmundt, D., Schnülle, V., Mattei, M.G., Thies, U. Biochim. Biophys. Acta (1995) [Pubmed]
  10. The oncogene qin codes for a transcriptional repressor. Li, J., Chang, H.W., Lai, E., Parker, E.J., Vogt, P.K. Cancer Res. (1995) [Pubmed]
  11. Functional cloning of the proto-oncogene brain factor-1 (BF-1) as a Smad-binding antagonist of transforming growth factor-beta signaling. Rodriguez, C., Huang, L.J., Son, J.K., McKee, A., Xiao, Z., Lodish, H.F. J. Biol. Chem. (2001) [Pubmed]
  12. Supplementary motor area activation preceding voluntary movement is detectable with a whole-scalp magnetoencephalography system. Erdler, M., Beisteiner, R., Mayer, D., Kaindl, T., Edward, V., Windischberger, C., Lindinger, G., Deecke, L. Neuroimage (2000) [Pubmed]
  13. Distribution of metronidazole in muscle tissue of patients with septic shock and its efficacy against Bacteroides fragilis in vitro. Karjagin, J., Pähkla, R., Karki, T., Starkopf, J. J. Antimicrob. Chemother. (2005) [Pubmed]
  14. Human PLU-1 Has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9. Tan, K., Shaw, A.L., Madsen, B., Jensen, K., Taylor-Papadimitriou, J., Freemont, P.S. J. Biol. Chem. (2003) [Pubmed]
  15. Human brain factor 1, a new member of the fork head gene family. Murphy, D.B., Wiese, S., Burfeind, P., Schmundt, D., Mattei, M.G., Schulz-Schaeffer, W., Thies, U. Genomics (1994) [Pubmed]
  16. Repression of CDC28 reduces the expression of the morphology-related transcription factors, Efg1p, Nrg1p, Rbf1p, Rim101p, Fkh2p and Tec1p and induces cell elongation in Candida albicans. Umeyama, T., Kaneko, A., Niimi, M., Uehara, Y. Yeast (2006) [Pubmed]
 
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