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Gene Review

BANF1  -  barrier to autointegration factor 1

Homo sapiens

Synonyms: BAF, BCRG1, BCRP1, Barrier-to-autointegration factor, Breakpoint cluster region protein 1, ...
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Disease relevance of BANF1


High impact information on BANF1


Biological context of BANF1


Anatomical context of BANF1


Associations of BANF1 with chemical compounds

  • The functional importance of MRP4 and BCRP in the urinary excretion of HCT and furosemide was investigated using gene knockout mice [14].
  • A G-CSF-R mutant was constructed in which tryptophan 650 was replaced by arginine and expressed in BAF3 cells (BAF/W650R) [15].
  • The breast cancer resistance protein (BCRP) is an ATP-binding cassette half transporter that confers resistance to anticancer drugs such as mitoxantrone, anthracyclines, topotecan, and SN-38 [16].
  • The V-ICEinh and BAF, two peptide inhibitors of cysteine aspartases, protected neurons in all three death paradigms [17].
  • A disparity was noted in the transport of rhodamine 123 among nine MXR/BCRP/ABCP-overexpressing cells studied; all demonstrated mitoxantrone transport, whereas only two effluxed rhodamine 123 [18].

Physical interactions of BANF1

  • An emerin mutant defective for binding to BAF in vitro failed to localize at the 'core' in vivo, and subsequently failed to localize at the reformed NE [11].
  • We report that BAF binds directly and selectively to linker histone H1.1 (among three subtypes tested) and core histone H3 with affinities of approximately 700 nm and approximately 100-200 nm, respectively, in vitro and in vivo [19].

Other interactions of BANF1

  • Sequence alignments identified a potential BAF-binding motif, characterized by the conserved residues Ser-Arg-Val, in MAN1-C and two other BAF-binding proteins [20].
  • Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1 [19].
  • Mutations at the bottom and top surfaces of the BAF dimer disrupted or enhanced, respectively, this binding and affected H1 and H3 similarly [19].
  • LAP2beta is a type II integral protein of the inner nuclear membrane, which binds to lamin B and the chromosomal protein BAF, and may link the nuclear membrane to the underlying lamina and provide docking sites for chromatin [21].
  • Emerin and lamin A together form stable complexes with either BAF or GCL in vitro [22].

Analytical, diagnostic and therapeutic context of BANF1


  1. Barrier-to-autointegration factor-like (BAF-L): a proposed regulator of BAF. Tifft, K.E., Segura-Totten, M., Lee, K.K., Wilson, K.L. Exp. Cell Res. (2006) [Pubmed]
  2. Both the structure and DNA binding function of the barrier-to-autointegration factor contribute to reconstitution of HIV type 1 integration in vitro. Harris, D., Engelman, A. J. Biol. Chem. (2000) [Pubmed]
  3. Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo. Bengtsson, L., Wilson, K.L. Mol. Biol. Cell (2006) [Pubmed]
  4. Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions. Mansharamani, M., Graham, D.R., Monie, D., Lee, K.K., Hildreth, J.E., Siliciano, R.F., Wilson, K.L. J. Virol. (2003) [Pubmed]
  5. Nuclear actin and actin-related proteins in chromatin remodeling. Olave, I.A., Reck-Peterson, S.L., Crabtree, G.R. Annu. Rev. Biochem. (2002) [Pubmed]
  6. Regulation of CSF1 promoter by the SWI/SNF-like BAF complex. Liu, R., Liu, H., Chen, X., Kirby, M., Brown, P.O., Zhao, K. Cell (2001) [Pubmed]
  7. BAF: roles in chromatin, nuclear structure and retrovirus integration. Segura-Totten, M., Wilson, K.L. Trends Cell Biol. (2004) [Pubmed]
  8. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. Segura-Totten, M., Kowalski, A.K., Craigie, R., Wilson, K.L. J. Cell Biol. (2002) [Pubmed]
  9. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. Cai, M., Huang, Y., Ghirlando, R., Wilson, K.L., Craigie, R., Clore, G.M. EMBO J. (2001) [Pubmed]
  10. Dissociation of emerin from barrier-to-autointegration factor is regulated through mitotic phosphorylation of emerin in a xenopus egg cell-free system. Hirano, Y., Segawa, M., Ouchi, F.S., Yamakawa, Y., Furukawa, K., Takeyasu, K., Horigome, T. J. Biol. Chem. (2005) [Pubmed]
  11. BAF is required for emerin assembly into the reforming nuclear envelope. Haraguchi, T., Koujin, T., Segura-Totten, M., Lee, K.K., Matsuoka, Y., Yoneda, Y., Wilson, K.L., Hiraoka, Y. J. Cell. Sci. (2001) [Pubmed]
  12. Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells. Shimi, T., Koujin, T., Segura-Totten, M., Wilson, K.L., Haraguchi, T., Hiraoka, Y. J. Struct. Biol. (2004) [Pubmed]
  13. The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype. Fairley, E.A., Riddell, A., Ellis, J.A., Kendrick-Jones, J. J. Cell. Sci. (2002) [Pubmed]
  14. Multidrug resistance-associated protein 4 is involved in the urinary excretion of hydrochlorothiazide and furosemide. Hasegawa, M., Kusuhara, H., Adachi, M., Schuetz, J.D., Takeuchi, K., Sugiyama, Y. J. Am. Soc. Nephrol. (2007) [Pubmed]
  15. Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G-CSF-mediated activation of signaling complexes of the p21ras route. Barge, R.M., de Koning, J.P., Pouwels, K., Dong, F., Löwenberg, B., Touw, I.P. Blood (1996) [Pubmed]
  16. Identification of a novel estrogen response element in the breast cancer resistance protein (ABCG2) gene. Ee, P.L., Kamalakaran, S., Tonetti, D., He, X., Ross, D.D., Beck, W.T. Cancer Res. (2004) [Pubmed]
  17. Multiple pathways of neuronal death induced by DNA-damaging agents, NGF deprivation, and oxidative stress. Park, D.S., Morris, E.J., Stefanis, L., Troy, C.M., Shelanski, M.L., Geller, H.M., Greene, L.A. J. Neurosci. (1998) [Pubmed]
  18. Acquired mutations in the MXR/BCRP/ABCP gene alter substrate specificity in MXR/BCRP/ABCP-overexpressing cells. Honjo, Y., Hrycyna, C.A., Yan, Q.W., Medina-Pérez, W.Y., Robey, R.W., van de Laar, A., Litman, T., Dean, M., Bates, S.E. Cancer Res. (2001) [Pubmed]
  19. Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1. de Oca, R.M., Lee, K.K., Wilson, K.L. J. Biol. Chem. (2005) [Pubmed]
  20. Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. Mansharamani, M., Wilson, K.L. J. Biol. Chem. (2005) [Pubmed]
  21. Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. Dechat, T., Vlcek, S., Foisner, R. J. Struct. Biol. (2000) [Pubmed]
  22. Nuclear membrane protein emerin: roles in gene regulation, actin dynamics and human disease. Wilson, K.L., Holaska, J.M., de Oca, R.M., Tifft, K., Zastrow, M., Segura-Totten, M., Mansharamani, M., Bengtsson, L. Novartis Found. Symp. (2005) [Pubmed]
  23. The barrier-to-autointegration protein is a host factor for HIV type 1 integration. Chen, H., Engelman, A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  24. An improved specimen table for the Balzers freeze etching system BAF 400. Wisse, D.M., Spies, F. Journal of microscopy. (1982) [Pubmed]
  25. Diagnostic signs of accommodative insufficiency. Cacho, P., García, A., Lara, F., Seguí, M.M. Optometry and vision science : official publication of the American Academy of Optometry. (2002) [Pubmed]
  26. Baf60c is essential for function of BAF chromatin remodelling complexes in heart development. Lickert, H., Takeuchi, J.K., Von Both, I., Walls, J.R., McAuliffe, F., Adamson, S.L., Henkelman, R.M., Wrana, J.L., Rossant, J., Bruneau, B.G. Nature (2004) [Pubmed]
  27. Role of the ABCG2 drug transporter in the resistance and oral bioavailability of a potent cyclin-dependent kinase/Aurora kinase inhibitor. Seamon, J.A., Rugg, C.A., Emanuel, S., Calcagno, A.M., Ambudkar, S.V., Middleton, S.A., Butler, J., Borowski, V., Greenberger, L.M. Mol. Cancer Ther. (2006) [Pubmed]
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