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Gene Review

Bex1  -  brain expressed gene 1

Mus musculus

Synonyms: AA407839, AU018692, Bex4, Brain-expressed X-linked protein 1 homolog, Protein BEX1, ...
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Disease relevance of Bex1

  • On the other hand, Bex1 folded 3-4 times better than the wtGFP or S65T in E. coli, and 10-20-fold or more than 95-fold better, respectively, in mammalian cells [1].
  • However, forced overexpression of Rex3 did not significantly affect proliferation or stress-induced apoptosis of transfected mouse hepatoma cells [2].

High impact information on Bex1

  • Bex1 knock out (Bex1-KO) mice appeared to develop normally and are fertile, but displayed a functional deficit in exercise performance compared to wild type (WT) mice [3].
  • Bex1-KO mice show altered muscle regeneration, and allow us to propose that the interaction of Bex1 with Ca(2+)/ CaM may be involved in skeletal muscle regeneration [3].
  • Together, these data establish Bex1 as a novel link between neurotrophin signaling, the cell cycle, and neuronal differentiation, and suggest that Bex1 may function by coordinating internal cellular states with the ability of cells to respond to external signals [4].
  • Human Bex1 and Bex2 have similar expression patterns in the central nervous system with high levels in pituitary, cerebellum, and temporal lobe, and Bex1 is widely expressed outside of the central nervous system with high expression in the liver [5].
  • Haploid parthenogenones display only very subtle alterations in the expression of most mRNAs but a consistent elevation in X-linked Bex1 mRNA expression [6].
  • The Bex1/Rex3 gene appears to be expressed preferentially from the maternal X chromosome in blastocysts, but from either X chromosome in later stage embryonic tissues and adult tissues [7].
  • The Bex1/Rex3 gene was recently identified as an X-linked gene that is differentially expressed between parthenogenetic and normal fertilized, preimplantation stage mouse embryos [7].

Biological context of Bex1

  • Through screening a human fetal brain cDNA library, a cDNA similar to the mouse Bex1 was isolated [8].
  • Thus, the Bex1/Rex3 gene does not appear to be regulated directly by genomic imprinting during the preimplantation period, just as it is not regulated by imprinting at later stages [7].

Anatomical context of Bex1

  • Bex1/2 immunoreactivity (ir) was primarily localized to neuronal cells within several regions of the brain, including the olfactory epithelium, bulb, peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus, median eminence, lateral hypothalamic area, thalamus, hippocampus, and cerebellum [9].
  • Expression data reveal that the Bex1/Rex3 gene is initially transcribed at the 2-cell stage, transiently induced at the 8-cell stage, and then increases in expression again at the blastocyst stage [7].
  • In primary mouse hepatocytes, expression of Rex3 increased while cells dedifferentiated in culture [2].

Associations of Bex1 with chemical compounds

  • The expression of the REX-2, REX-3, pyruvate kinase, glutathione S-transferase and GLUT 3 genes is reduced by RACT to the same extent in F9 RARgamma-/- and RARalpha-/- lines as in F9-Wt [10].

Other interactions of Bex1

  • Bex1 and Calmodulin (CaM) interact in a calcium-dependent manner [3].
  • In isoleucine-deprived cells, which are growth arrested but do not differentiate, the steady state mRNA levels of genes Rex 2, Rex 3, pyruvate kinase and GLUT 3 are not reduced, in contrast to cyclin D3 and glutathione S-transferase [10].

Analytical, diagnostic and therapeutic context of Bex1

  • The specificity of the antiserum was characterized by immunoprecipitation and Western blots of tissue and transfected cell extracts and by immunocytochemical analyses of cells transfected with either Bex1 or Bex2 [11].
  • Using a peptide titration series, we have identified this cleft as the binding surface for a peptide derived from the Bex1 protein [12].
  • Rex3 mRNA was determined in primary hepatocytes in culture by real-time PCR [2].


  1. Green fluorescent protein variants fold differentially in prokaryotic and eukaryotic cells. Sacchetti, A., Cappetti, V., Marra, P., Dell'Arciprete, R., El Sewedy, T., Crescenzi, C., Alberti, S. J. Cell. Biochem. Suppl. (2001) [Pubmed]
  2. Rex3 (reduced in expression 3) as a new tumor marker in mouse hepatocarcinogenesis. Braeuning, A., Jaworski, M., Schwarz, M., Köhle, C. Toxicology (2006) [Pubmed]
  3. Bex1 knock out mice show altered skeletal muscle regeneration. Koo, J.H., Smiley, M.A., Lovering, R.M., Margolis, F.L. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  4. Bex1, a novel interactor of the p75 neurotrophin receptor, links neurotrophin signaling to the cell cycle. Vilar, M., Murillo-Carretero, M., Mira, H., Magnusson, K., Besset, V., Ibáñez, C.F. EMBO J. (2006) [Pubmed]
  5. Characterization of the Bex gene family in humans, mice, and rats. Alvarez, E., Zhou, W., Witta, S.E., Freed, C.R. Gene (2005) [Pubmed]
  6. Comparison of gene expression during preimplantation development between diploid and haploid mouse embryos. Latham, K.E., Akutsu, H., Patel, B., Yanagimachi, R. Biol. Reprod. (2002) [Pubmed]
  7. Trophectoderm-specific expression of the X-linked Bex1/Rex3 gene in preimplantation stage mouse embryos. Williams, J.W., Hawes, S.M., Patel, B., Latham, K.E. Mol. Reprod. Dev. (2002) [Pubmed]
  8. Cloning and expression pattern of a spermatogenesis-related gene, BEX1, mapped to chromosome Xq22. Yang, Q.S., Xia, F., Gu, S.H., Yuan, H.L., Chen, J.Z., Yang, Q.S., Ying, K., Xie, Y., Mao, Y.M. Biochem. Genet. (2002) [Pubmed]
  9. Immunolocalization of Bex protein in the mouse brain and olfactory system. Koo, J.H., Saraswati, M., Margolis, F.L. J. Comp. Neurol. (2005) [Pubmed]
  10. Characterization of genes which exhibit reduced expression during the retinoic acid-induced differentiation of F9 teratocarcinoma cells: involvement of cyclin D3 in RA-mediated growth arrest. Faria, T.N., LaRosa, G.J., Wilen, E., Liao, J., Gudas, L.J. Mol. Cell. Endocrinol. (1998) [Pubmed]
  11. Immunolocalization of Bex protein in the mouse brain and olfactory system. Koo, J.H., Saraswati, M., Margolis, F.L. J. Comp. Neurol. (2005) [Pubmed]
  12. Olfactory marker protein (OMP) exhibits a beta-clam fold in solution: implications for target peptide interaction and olfactory signal transduction. Baldisseri, D.M., Margolis, J.W., Weber, D.J., Koo, J.H., Margolis, F.L. J. Mol. Biol. (2002) [Pubmed]
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