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Chemical Compound Review

boraniumyl     boron(+1) trihydride cation

Synonyms: CHEBI:30155, BH3(.+), [BH3](.+), trihydridoboron(.1+)
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Disease relevance of boraniumyl

  • Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins [1].
  • Using polymerase chain reaction-based suppression subtractive hybridization to find genes that are differentially expressed in hypoxia, we identified the BH3-only Bcl-2 family protein Noxa [2].
  • BNIP1, a member of the BH3-only protein family, was first discovered as one of the proteins that are capable of interacting with the antiapoptotic adenovirus E1B 19-kDa protein [3].
  • The Bik BH3-only protein is induced in estrogen-starved and antiestrogen-exposed breast cancer cells and provokes apoptosis [4].
  • Moreover, whereas loss of the BH3-only protein Bim rescued mice lacking the prosurvival protein Bcl-2 from fatal polycystic kidney disease and lymphopenia, loss of Bik did not [5].

High impact information on boraniumyl

  • Control of apoptosis in the immune system: Bcl-2, BH3-only proteins and more [6].
  • BID and BAD possess the minimal death domain BH3, and the phosphorylation of BAD connects proximal survival signals to the BCL-2 family [7].
  • Here, we demonstrated that the BH3-only BID protein partially localizes to the nucleus in healthy cells, is important for apoptosis induced by DNA damage, and is phosphorylated following induction of double-strand breaks in DNA [8].
  • Our previous data demonstrated a role for BH3-only BID in maintaining myeloid homeostasis and suppressing leukemogenesis [9].
  • Nur77 binding induces a Bcl-2 conformational change that exposes its BH3 domain, resulting in conversion of Bcl-2 from a protector to a killer [10].

Chemical compound and disease context of boraniumyl


Biological context of boraniumyl

  • The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain [16].
  • The carboxyl-terminal Bcl-2 cleavage product triggered cell death and accelerated Sindbis virus-induced apoptosis, which was dependent on the BH3 homology and transmembrane domains of Bcl-2 [17].
  • Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis [18].
  • These interactions require the Bak BH3 domain, which is also necessary for Bak dimerization and killing activity [19].
  • Mutagenesis revealed that an intact BH3 domain of BID was required to bind the BH1 domain of either BCL-2 or BAX [20].

Anatomical context of boraniumyl

  • We conclude that mitochondrial protein release in apoptosis can be mediated by supramolecular openings in the outer mitochondrial membrane, promoted by BH3/Bax/lipid interaction and directly inhibited by Bcl-x(L) [21].
  • It appears two criteria must be met for proapoptotic function within the BCL2 family: targeting of molecules to intracellular membranes, and exposure of the BH3 death domain [22].
  • Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis by binding via their BH3 domain to prosurvival relatives, while the proapoptotic Bax and Bak have an essential downstream role involving permeabilization of organellar membranes and induction of caspase activation [19].
  • We found that naive human T cells after mitogenic activation, apart from expected protective Bcl-2 members, also rapidly upregulate the BH3-only protein Noxa in a p53-independent fashion [23].
  • Besides having this derepression function, the Bid and Bim peptides activated Bax directly and were the only BH3 peptides tested that could potently induce cytochrome c release from mitochondria in cultured cells [24].

Associations of boraniumyl with other chemical compounds

  • The BH3 only proteins, Bad and Bim, were also part of the death pathway repressed by IL-7 [25].
  • Hrk lacks conserved BH1 and BH2 regions and significant homology to Bcl-2 family members or any other protein, except for a stretch of eight amino acids that exhibits high homology with BH3 regions [26].
  • Notably, a highly conserved leucine residue in the BH3 domain of BNIP1 plays an important role not only in the induction of apoptosis but also in the binding of alpha-SNAP, an adaptor that serves as a link between the chaperone ATPase NSF and SNAREs [3].
  • The C-terminal hydrophobic tails of two Bcl-x(L) molecules are involved in homodimer formation, and analysis of mutants demonstrates that the C-terminal lysine residue and the G138 residue lining the BH3-binding pocket are required for homodimerization [27].
  • [Ca(2+)](er) proved coordinate with the capacity of BCL-2 to bind proapoptotic BH3-only members, further integrating the apoptotic pathway and Ca(2+) modulation [28].

Gene context of boraniumyl

  • Peptide mass fingerprinting identified this protein as Bid, a BH3 domain-containing protein known to interact with both Bcl2 and Bax [29].
  • These results suggest that neither activation of BH3-only proteins nor suppression of pro-survival Bcl-2 proteins is sufficient to kill cells in the absence of both Bax and Bak [30].
  • The BH3-only proteins Bim and Bad bind to the antiapoptotic Bcl-2 proteins and induce apoptosis in wild-type cells and cells from either bax(-/-) or bak(-/-) animals [30].
  • Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function [31].
  • These interactions have been considered promiscuous, but our analysis of the affinity of eight BH3 peptides for five Bcl-2-like proteins has revealed that the interactions vary over 10,000-fold in affinity, and accordingly, only certain protein pairs associate inside cells [31].

Analytical, diagnostic and therapeutic context of boraniumyl

  • Previous gene-targeting studies indicated that Bim, a BH3-only death activator, regulates total blood cell number [32].
  • These results suggest that ligation of a proapoptotic BH3-only protein alters the conformation of Bcl-w, enhances membrane association, and neutralizes its survival function [33].
  • An extensive site-directed mutagenesis of BH3 revealed that substitutions along the hydrophobic face of BH3, especially charged substitutions, had the greatest affects on dimerization patterns and death agonist activity [34].
  • However, glucocorticoid resistance was associated with profoundly attenuated induction of the BH3-only proapoptotic protein, Bim, when xenograft cells were exposed to dexamethasone [35].
  • Moreover, susceptibility to c-Myc-induced apoptosis can be restored in bax-deficient cells by ectopic expression of Bax or by microinjection of a peptide comprising a minimal BH3 domain [36].


  1. Chlamydia inhibit host cell apoptosis by degradation of proapoptotic BH3-only proteins. Fischer, S.F., Vier, J., Kirschnek, S., Klos, A., Hess, S., Ying, S., Häcker, G. J. Exp. Med. (2004) [Pubmed]
  2. BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha. Kim, J.Y., Ahn, H.J., Ryu, J.H., Suk, K., Park, J.H. J. Exp. Med. (2004) [Pubmed]
  3. Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion. Nakajima, K., Hirose, H., Taniguchi, M., Kurashina, H., Arasaki, K., Nagahama, M., Tani, K., Yamamoto, A., Tagaya, M. EMBO J. (2004) [Pubmed]
  4. The Bik BH3-only protein is induced in estrogen-starved and antiestrogen-exposed breast cancer cells and provokes apoptosis. Hur, J., Chesnes, J., Coser, K.R., Lee, R.S., Geck, P., Isselbacher, K.J., Shioda, T. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. Proapoptotic BH3-only Bcl-2 family member Bik/Blk/Nbk is expressed in hemopoietic and endothelial cells but is redundant for their programmed death. Coultas, L., Bouillet, P., Stanley, E.G., Brodnicki, T.C., Adams, J.M., Strasser, A. Mol. Cell. Biol. (2004) [Pubmed]
  6. Control of apoptosis in the immune system: Bcl-2, BH3-only proteins and more. Marsden, V.S., Strasser, A. Annu. Rev. Immunol. (2003) [Pubmed]
  7. BCL-2 family: regulators of cell death. Chao, D.T., Korsmeyer, S.J. Annu. Rev. Immunol. (1998) [Pubmed]
  8. Proapoptotic BID is an ATM effector in the DNA-damage response. Kamer, I., Sarig, R., Zaltsman, Y., Niv, H., Oberkovitz, G., Regev, L., Haimovich, G., Lerenthal, Y., Marcellus, R.C., Gross, A. Cell (2005) [Pubmed]
  9. A role for proapoptotic BID in the DNA-damage response. Zinkel, S.S., Hurov, K.E., Ong, C., Abtahi, F.M., Gross, A., Korsmeyer, S.J. Cell (2005) [Pubmed]
  10. Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Lin, B., Kolluri, S.K., Lin, F., Liu, W., Han, Y.H., Cao, X., Dawson, M.I., Reed, J.C., Zhang, X.K. Cell (2004) [Pubmed]
  11. Enhanced Killing of Melanoma Cells by Simultaneously Targeting Mcl-1 and NOXA. Qin, J.Z., Xin, H., Sitailo, L.A., Denning, M.F., Nickoloff, B.J. Cancer Res. (2006) [Pubmed]
  12. The Secreted Protease Factor CPAF Is Responsible for Degrading Pro-apoptotic BH3-only Proteins in Chlamydia trachomatis-infected Cells. Pirbhai, M., Dong, F., Zhong, Y., Pan, K.Z., Zhong, G. J. Biol. Chem. (2006) [Pubmed]
  13. Lovastatin-induced up-regulation of the BH3-only protein, Bim, and cell death in glioblastoma cells. Jiang, Z., Zheng, X., Lytle, R.A., Higashikubo, R., Rich, K.M. J. Neurochem. (2004) [Pubmed]
  14. Beyond peroxisome proliferator-activated receptor gamma signaling: the multi-facets of the antitumor effect of thiazolidinediones. Weng, J.R., Chen, C.Y., Pinzone, J.J., Ringel, M.D., Chen, C.S. Endocr. Relat. Cancer (2006) [Pubmed]
  15. The role of various Bcl-2 domains in the anti-proliferative effect and modulation of cellular glutathione levels: a prominent role for the BH4 domain. Hoetelmans, R.W., Vahrmeijer, A.L., van Vlierberghe, R.L., Keijzer, R., van de Velde, C.J., Mulder, G.J., Van Dierendonck, J.H. Cell Prolif. (2003) [Pubmed]
  16. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Chou, J.J., Li, H., Salvesen, G.S., Yuan, J., Wagner, G. Cell (1999) [Pubmed]
  17. Conversion of Bcl-2 to a Bax-like death effector by caspases. Cheng, E.H., Kirsch, D.G., Clem, R.J., Ravi, R., Kastan, M.B., Bedi, A., Ueno, K., Hardwick, J.M. Science (1997) [Pubmed]
  18. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Puthalakath, H., Villunger, A., O'Reilly, L.A., Beaumont, J.G., Coultas, L., Cheney, R.E., Huang, D.C., Strasser, A. Science (2001) [Pubmed]
  19. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Willis, S.N., Chen, L., Dewson, G., Wei, A., Naik, E., Fletcher, J.I., Adams, J.M., Huang, D.C. Genes Dev. (2005) [Pubmed]
  20. BID: a novel BH3 domain-only death agonist. Wang, K., Yin, X.M., Chao, D.T., Milliman, C.L., Korsmeyer, S.J. Genes Dev. (1996) [Pubmed]
  21. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Kuwana, T., Mackey, M.R., Perkins, G., Ellisman, M.H., Latterich, M., Schneiter, R., Green, D.R., Newmeyer, D.D. Cell (2002) [Pubmed]
  22. Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. McDonnell, J.M., Fushman, D., Milliman, C.L., Korsmeyer, S.J., Cowburn, D. Cell (1999) [Pubmed]
  23. The Noxa/Mcl-1 axis regulates susceptibility to apoptosis under glucose limitation in dividing T cells. Alves, N.L., Derks, I.A., Berk, E., Spijker, R., van Lier, R.A., Eldering, E. Immunity (2006) [Pubmed]
  24. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Kuwana, T., Bouchier-Hayes, L., Chipuk, J.E., Bonzon, C., Sullivan, B.A., Green, D.R., Newmeyer, D.D. Mol. Cell (2005) [Pubmed]
  25. Bax deficiency partially corrects interleukin-7 receptor alpha deficiency. Khaled, A.R., Li, W.Q., Huang, J., Fry, T.J., Khaled, A.S., Mackall, C.L., Muegge, K., Young, H.A., Durum, S.K. Immunity (2002) [Pubmed]
  26. harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L). Inohara, N., Ding, L., Chen, S., Núñez, G. EMBO J. (1997) [Pubmed]
  27. Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers. Jeong, S.Y., Gaume, B., Lee, Y.J., Hsu, Y.T., Ryu, S.W., Yoon, S.H., Youle, R.J. EMBO J. (2004) [Pubmed]
  28. Phosphorylation of BCL-2 regulates ER Ca2+ homeostasis and apoptosis. Bassik, M.C., Scorrano, L., Oakes, S.A., Pozzan, T., Korsmeyer, S.J. EMBO J. (2004) [Pubmed]
  29. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Luo, X., Budihardjo, I., Zou, H., Slaughter, C., Wang, X. Cell (1998) [Pubmed]
  30. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Zong, W.X., Lindsten, T., Ross, A.J., MacGregor, G.R., Thompson, C.B. Genes Dev. (2001) [Pubmed]
  31. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Chen, L., Willis, S.N., Wei, A., Smith, B.J., Fletcher, J.I., Hinds, M.G., Colman, P.M., Day, C.L., Adams, J.M., Huang, D.C. Mol. Cell (2005) [Pubmed]
  32. Cytokines direct the regulation of bim mRNA stability by heat-shock cognate protein 70. Matsui, H., Asou, H., Inaba, T. Mol. Cell (2007) [Pubmed]
  33. Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity. Wilson-Annan, J., O'Reilly, L.A., Crawford, S.A., Hausmann, G., Beaumont, J.G., Parma, L.P., Chen, L., Lackmann, M., Lithgow, T., Hinds, M.G., Day, C.L., Adams, J.M., Huang, D.C. J. Cell Biol. (2003) [Pubmed]
  34. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing. Wang, K., Gross, A., Waksman, G., Korsmeyer, S.J. Mol. Cell. Biol. (1998) [Pubmed]
  35. Dexamethasone resistance in B-cell precursor childhood acute lymphoblastic leukemia occurs downstream of ligand-induced nuclear translocation of the glucocorticoid receptor. Bachmann, P.S., Gorman, R., Mackenzie, K.L., Lutze-Mann, L., Lock, R.B. Blood (2005) [Pubmed]
  36. c-Myc functionally cooperates with Bax to induce apoptosis. Juin, P., Hunt, A., Littlewood, T., Griffiths, B., Swigart, L.B., Korsmeyer, S., Evan, G. Mol. Cell. Biol. (2002) [Pubmed]
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