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Banf1  -  barrier to autointegration factor 1

Mus musculus

Synonyms: Baf, Barrier-to-autointegration factor, Bcrp1, Breakpoint cluster region protein 1, C78287, ...
 
 
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Disease relevance of Banf1

  • Data base search identified the HB antigen as the barrier-to-autointegration factor, a cellular protein implicated in the cellular cycle that blocks autointegration and promotes intermolecular integration of retrovirus such as the Moloney murine leukemia and the human immunodeficiency type 1 virus [1].
  • However, after exposure of NIH 3T3 cells to hydroxyurea (HU), a compound known to increase AAV-mediated transduction in general, virions were detected in late endosomes and lysosomes, and these cells became sensitive to Baf-mediated inhibition of transduction [2].
  • We have demonstrated that barrier-to-autointegration factor (BAF) blocks the autointegration of Moloney murine leukemia virus (MoMLV) PICs in vitro [3].
  • SP cells can be isolated by dual-wavelength flow cytometry because of their capacity to efflux Hoechst dye, a process mediated by the ATP-binding cassette transporter breast cancer resistance protein (Bcrp) 1 [4].
 

High impact information on Banf1

  • Barrier-to-autointegration factor, a cellular protein that blocks autointegration of Moloney murine leukemia virus DNA, also plays an indirect role in generating the footprints at the ends of the viral DNA [5].
  • Bcrp-1 expression was similarly detected in SP- and MP-CD34(-)KSL cells, suggesting that the SP phenotype is regulated not only by Bcrp-1, but also by other factors [6].
  • Withdrawal of STI571 for varying lengths of time from cultures of 3 resistant lines (K562-r, KCL22-r, and Baf/BCR-ABL-r1) did not restore sensitivity to the inhibitor [7].
  • 'Side Population' cells in adult mouse testis express Bcrp1 gene and are enriched in spermatogonia and germinal stem cells [8].
  • Although our studies did not identify a causative Baf mutation in retinopathies, we suggest that Baf may contribute to the phenotype of a photoreceptor degenerative disease by modifying the activity of Crx [9].
 

Chemical compound and disease context of Banf1

 

Biological context of Banf1

  • One of the identified clones encodes Baf (barrier to autointegration factor), which was previously shown to have a role in mitosis and retroviral integration [9].
  • In view of the ubiquitous expression of Baf, we hypothesize that it may play a role in regulating tissue- or cell type-specific gene expression by interacting with homeodomain transcription factors [9].
  • Consistent with this role for Baf, an E80A mutation of CRX associated with cone-rod dystrophy has a higher than normal transactivation potency but a reduced interaction with Baf [9].
 

Anatomical context of Banf1

  • The Baf protein is detectable in all nuclear layers of the mouse retina, including the photoreceptors and the bipolar cells where Crx is expressed [9].
  • Moreover, treatment of cells with bafilomycin A1 (Baf), an inhibitor of the vacuolar H(+)-ATPase and therefore of endosomal-lysosomal acidification, decreased the transduction of 293 cells with a concomitant decrease in nuclear trafficking of AAV but had no effect on NIH 3T3 cells [2].
  • Surface marker analysis revealed lung SP cells to be stem cell antigen 1 positive, Bcrp1 positive, lineage marker negative, and heterogeneous at the CD45 locus [4].
  • We confirmed the expression of Bcrp1 in primary bronchial smooth muscle cell cultures (BSMC) and in lavaged distal airway cells, but neither possessed the capacity to efflux Hoechst dye [4].
 

Associations of Banf1 with chemical compounds

 

Other interactions of Banf1

  • Additional biochemical assays provided supporting evidence for a Baf-Crx interaction [9].
 

Analytical, diagnostic and therapeutic context of Banf1

  • We, therefore, employed nonisotopic in situ hybridization and immunostaining for Bcrp1 as a strategy to localize these cells in vivo [4].

References

  1. Identification of the autoantigen HB as the barrier-to-autointegration factor. Forné, I., Carrascal, M., Martinez-Lostao, L., Abian, J., Rodriguez-Sánchez, J.L., Juarez, C. J. Biol. Chem. (2003) [Pubmed]
  2. Adeno-associated virus type 2-mediated gene transfer: altered endocytic processing enhances transduction efficiency in murine fibroblasts. Hansen, J., Qing, K., Srivastava, A. J. Virol. (2001) [Pubmed]
  3. Regulatory mechanisms by which barrier-to-autointegration factor blocks autointegration and stimulates intermolecular integration of Moloney murine leukemia virus preintegration complexes. Suzuki, Y., Craigie, R. J. Virol. (2002) [Pubmed]
  4. Side population cells and Bcrp1 expression in lung. Summer, R., Kotton, D.N., Sun, X., Ma, B., Fitzsimmons, K., Fine, A. Am. J. Physiol. Lung Cell Mol. Physiol. (2003) [Pubmed]
  5. Footprints on the viral DNA ends in moloney murine leukemia virus preintegration complexes reflect a specific association with integrase. Wei, S.Q., Mizuuchi, K., Craigie, R. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  6. Non-side-population hematopoietic stem cells in mouse bone marrow. Morita, Y., Ema, H., Yamazaki, S., Nakauchi, H. Blood (2006) [Pubmed]
  7. Restoration of sensitivity to STI571 in STI571-resistant chronic myeloid leukemia cells. Tipping, A.J., Mahon, F.X., Lagarde, V., Goldman, J.M., Melo, J.V. Blood (2001) [Pubmed]
  8. 'Side Population' cells in adult mouse testis express Bcrp1 gene and are enriched in spermatogonia and germinal stem cells. Lassalle, B., Bastos, H., Louis, J.P., Riou, L., Testart, J., Dutrillaux, B., Fouchet, P., Allemand, I. Development (2004) [Pubmed]
  9. Barrier to autointegration factor interacts with the cone-rod homeobox and represses its transactivation function. Wang, X., Xu, S., Rivolta, C., Li, L.Y., Peng, G.H., Swain, P.K., Sung, C.H., Swaroop, A., Berson, E.L., Dryja, T.P., Chen, S. J. Biol. Chem. (2002) [Pubmed]
  10. Coordinated expression of multidrug resistance-associated proteins (Mrps) in mouse liver during toxicant-induced injury. Aleksunes, L.M., Scheffer, G.L., Jakowski, A.B., Pruimboom-Brees, I.M., Manautou, J.E. Toxicol. Sci. (2006) [Pubmed]
  11. Differential interaction with endocytic and exocytic pathways distinguish parasitophorous vacuoles of Coxiella burnetii and Chlamydia trachomatis. Heinzen, R.A., Scidmore, M.A., Rockey, D.D., Hackstadt, T. Infect. Immun. (1996) [Pubmed]
 
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