The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Bax  -  Bcl2-associated X protein

Rattus norvegicus

Synonyms: Apoptosis regulator BAX
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Bax

  • The peak of Bax expression and TUNEL+ staining in osteocytes was observed immediately at the microcrack locus, which is where bone resorption occurs in this system; in contrast, Bcl-2 expression, the antiapoptotic signal, reached its greatest level at some distance (1-2 mm) from microcracks [1].
  • CONCLUSIONS: Our findings suggest that the changes in the ratio of Bax to Bcl-2 may contribute to the caspase-3 activation and the modulation of renal apoptosis associated with renal inflammation, tubular atrophy and renal fibrosis in experimental glomerulonephritis [2].
  • A shift in the Bax/Bcl-2 balance may activate caspase-3 and modulate apoptosis in experimental glomerulonephritis [2].
  • Here, using the nephrotoxic nephritis (NTN) model, we evaluated Bax/Bcl-2 in relation to changes in the apoptosis co-ordination enzyme, caspase-3 [2].
  • Results suggest that germ cell apoptosis following ischemia/reperfusion of the rat testis is initiated through the mitochondria-associated molecule Bax as well as Fas-FasL interactions [3].

Psychiatry related information on Bax


High impact information on Bax

  • In agreement with this, VDAC1-deficient mitochondria from a mutant yeast did not exhibit a Bax/Bak-induced loss in membrane potential and cytochrome c release, both of which were inhibited by Bcl-x(L) [6].
  • These findings indicate that Bcl-2 can interfere with Bax killing downstream of and independently of cytochrome c release [7].
  • The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein [8].
  • In mammalian cells, oligomycin also inhibited Bax-induced apoptosis and activation of cell death proteases [9].
  • The proapoptotic mammalian protein Bax associates with mitochondrial membranes and confers a lethal phenotype when expressed in yeast [9].

Chemical compound and disease context of Bax


Biological context of Bax


Anatomical context of Bax


Associations of Bax with chemical compounds


Physical interactions of Bax


Enzymatic interactions of Bax


Regulatory relationships of Bax

  • Bcl-2 changes conformation to inhibit Bax oligomerization [15].
  • Thus, p53 induces apoptosis in part through Bax and Bak, and even an incomplete inhibition of this mitochondrial checkpoint may be sufficient to confer resistance to cell death [29].
  • These results suggest that the JNK signaling pathway is involved in ischemia-induced neuronal apoptosis by stimulation, at least in part, of Bax translocation to the mitochondria, in which BimL is likely regulated by JNK as a downstream substrate for transmission of apoptotic signals to Bax [30].
  • These findings indicate that Rho-kinase inhibition induces neointimal smooth muscle cell apoptosis through Bax upregulation, resulting in reduced neointima formation [31].
  • Myc potentiates apoptosis by stimulating Bax activity at the mitochondria [32].
  • Bax mRNA is increased by RhoA, indicating transcriptional regulation, and the ability of a dominant negative p53 mutant to block Bax up-regulation implicates p53 in this response [33].

Other interactions of Bax

  • In transfected cells and isolated mitochondria, Bcl-2, but not the inactive point mutants Bcl-2-G145A and Bcl-2-V159D, undergoes a conformation change in the mitochondrial membrane in response to apoptotic agonists such as tBid and Bax [15].
  • Selective activation of the c-Jun N-terminal kinase (JNK) pathway fails to elicit Bax activation or apoptosis unless the phosphoinositide 3'-kinase (PI3K) pathway is inhibited [24].
  • Our results demonstrate p53 and Bax as early components in NO. and O2(-)-induced rat MC apoptosis and point to the NO./O2- interaction as a naturally occurring cell defense mechanism [34].
  • After high-intensity irradiation, we observed decreased bcl-w and bcl-2 mRNA with increased Bcl-2 protein in the cytosolic fraction, whereas the Bax protein remained in scattered ischaemic cells in the ring lesion and the region at risk that corresponded with release of Smac/DIABLO from mitochondria to the cytosol at 1-24 h [35].
  • Hsp60 interacted with Bcl-xl and Bax in the cardiomyocytes in vivo [36].

Analytical, diagnostic and therapeutic context of Bax


  1. Spatial distribution of Bax and Bcl-2 in osteocytes after bone fatigue: complementary roles in bone remodeling regulation? Verborgt, O., Tatton, N.A., Majeska, R.J., Schaffler, M.B. J. Bone Miner. Res. (2002) [Pubmed]
  2. A shift in the Bax/Bcl-2 balance may activate caspase-3 and modulate apoptosis in experimental glomerulonephritis. Yang, B., Johnson, T.S., Thomas, G.L., Watson, P.F., Wagner, B., Furness, P.N., El Nahas, A.M. Kidney Int. (2002) [Pubmed]
  3. Molecular pathway of germ cell apoptosis following ischemia/reperfusion of the rat testis. Lysiak, J.J., Turner, S.D., Turner, T.T. Biol. Reprod. (2000) [Pubmed]
  4. Diabetes induced erectile dysfunction and apoptosis in penile crura are recovered by insulin treatment in rats. Yamanaka, M., Shirai, M., Shiina, H., Tanaka, Y., Tsujimura, A., Matsumiya, K., Okuyama, A., Dahiya, R. J. Urol. (2003) [Pubmed]
  5. Bax expression in mammalian neurons undergoing apoptosis, and in Alzheimer's disease hippocampus. MacGibbon, G.A., Lawlor, P.A., Sirimanne, E.S., Walton, M.R., Connor, B., Young, D., Williams, C., Gluckman, P., Faull, R.L., Hughes, P., Dragunow, M. Brain Res. (1997) [Pubmed]
  6. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Shimizu, S., Narita, M., Tsujimoto, Y. Nature (1999) [Pubmed]
  7. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Rossé, T., Olivier, R., Monney, L., Rager, M., Conus, S., Fellay, I., Jansen, B., Borner, C. Nature (1998) [Pubmed]
  8. The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein. Han, J., Sabbatini, P., Perez, D., Rao, L., Modha, D., White, E. Genes Dev. (1996) [Pubmed]
  9. The Mitochondrial F0F1-ATPase proton pump is required for function of the proapoptotic protein Bax in yeast and mammalian cells. Matsuyama, S., Xu, Q., Velours, J., Reed, J.C. Mol. Cell (1998) [Pubmed]
  10. Ordering of ceramide formation, caspase activation, and Bax/Bcl-2 expression during etoposide-induced apoptosis in C6 glioma cells. Sawada, M., Nakashima, S., Banno, Y., Yamakawa, H., Hayashi, K., Takenaka, K., Nishimura, Y., Sakai, N., Nozawa, Y. Cell Death Differ. (2000) [Pubmed]
  11. Celecoxib-induced apoptosis in rat cholangiocarcinoma cells mediated by Akt inactivation and Bax translocation. Zhang, Z., Lai, G.H., Sirica, A.E. Hepatology (2004) [Pubmed]
  12. Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury. Saikumar, P., Dong, Z., Patel, Y., Hall, K., Hopfer, U., Weinberg, J.M., Venkatachalam, M.A. Oncogene (1998) [Pubmed]
  13. Influence of Bax or Bcl-2 overexpression on the ceramide-dependent apoptotic pathway in glioma cells. Sawada, M., Nakashima, S., Banno, Y., Yamakawa, H., Takenaka, K., Shinoda, J., Nishimura, Y., Sakai, N., Nozawa, Y. Oncogene (2000) [Pubmed]
  14. Protein Kinase C-Dependent Mitochondrial Translocation of Proapoptotic Protein Bax on Activation of Inducible Nitric-Oxide Synthase in Rostral Ventrolateral Medulla Mediates Cardiovascular Depression during Experimental Endotoxemia. Chan, J.Y., Chang, A.Y., Wang, L.L., Ou, C.C., Chan, S.H. Mol. Pharmacol. (2007) [Pubmed]
  15. Bcl-2 changes conformation to inhibit Bax oligomerization. Dlugosz, P.J., Billen, L.P., Annis, M.G., Zhu, W., Zhang, Z., Lin, J., Leber, B., Andrews, D.W. EMBO J. (2006) [Pubmed]
  16. Bax affects intracellular Ca2+ stores and induces Ca2+ wave propagation. Carvalho, A.C., Sharpe, J., Rosenstock, T.R., Teles, A.F., Youle, R.J., Smaili, S.S. Cell Death Differ. (2004) [Pubmed]
  17. Glucose-dependent insulinotropic polypeptide (GIP) stimulation of pancreatic beta-cell survival is dependent upon phosphatidylinositol 3-kinase (PI3K)/protein kinase B (PKB) signaling, inactivation of the forkhead transcription factor Foxo1, and down-regulation of bax expression. Kim, S.J., Winter, K., Nian, C., Tsuneoka, M., Koda, Y., McIntosh, C.H. J. Biol. Chem. (2005) [Pubmed]
  18. Distinct domains control the addressing and the insertion of Bax into mitochondria. Cartron, P.F., Arokium, H., Oliver, L., Meflah, K., Manon, S., Vallette, F.M. J. Biol. Chem. (2005) [Pubmed]
  19. Bid, but not Bax, regulates VDAC channels. Rostovtseva, T.K., Antonsson, B., Suzuki, M., Youle, R.J., Colombini, M., Bezrukov, S.M. J. Biol. Chem. (2004) [Pubmed]
  20. Altered signaling and regulatory mechanisms of apoptosis in focal and segmental glomerulosclerosis. Wang, W., Tzanidis, A., Divjak, M., Thomson, N.M., Stein-Oakley, A.N. J. Am. Soc. Nephrol. (2001) [Pubmed]
  21. Cytochrome c release from mitochondria proceeds by a two-step process. Ott, M., Robertson, J.D., Gogvadze, V., Zhivotovsky, B., Orrenius, S. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  22. Cancer cell sensitization to fas-mediated apoptosis by sodium butyrate. Bonnotte, B., Favre, N., Reveneau, S., Micheau, O., Droin, N., Garrido, C., Fontana, A., Chauffert, B., Solary, E., Martin, F. Cell Death Differ. (1998) [Pubmed]
  23. Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells. Weng, C., Li, Y., Xu, D., Shi, Y., Tang, H. J. Biol. Chem. (2005) [Pubmed]
  24. Selective activation of the c-Jun N-terminal kinase (JNK) pathway fails to elicit Bax activation or apoptosis unless the phosphoinositide 3'-kinase (PI3K) pathway is inhibited. Molton, S.A., Todd, D.E., Cook, S.J. Oncogene (2003) [Pubmed]
  25. Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes. Adachi, M., Higuchi, H., Miura, S., Azuma, T., Inokuchi, S., Saito, H., Kato, S., Ishii, H. Am. J. Physiol. Gastrointest. Liver Physiol. (2004) [Pubmed]
  26. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. Desagher, S., Osen-Sand, A., Nichols, A., Eskes, R., Montessuit, S., Lauper, S., Maundrell, K., Antonsson, B., Martinou, J.C. J. Cell Biol. (1999) [Pubmed]
  27. Activated JNK brings about accelerated apoptosis of Bcl-2-overexpressing C6 glioma cells on treatment with tamoxifen. Moodbidri, M.S., Shirsat, N.V. J. Neurochem. (2005) [Pubmed]
  28. Suppression of mitochondria-dependent neutrophil apoptosis with thermal injury. Hu, Z., Sayeed, M.M. Am. J. Physiol., Cell Physiol. (2004) [Pubmed]
  29. Regulation of the mitochondrial checkpoint in p53-mediated apoptosis confers resistance to cell death. Henry, H., Thomas, A., Shen, Y., White, E. Oncogene (2002) [Pubmed]
  30. The c-Jun N-terminal protein kinase signaling pathway mediates Bax activation and subsequent neuronal apoptosis through interaction with Bim after transient focal cerebral ischemia. Okuno, S., Saito, A., Hayashi, T., Chan, P.H. J. Neurosci. (2004) [Pubmed]
  31. Rho-kinase inhibition reduces neointima formation after vascular injury by enhancing Bax expression and apoptosis. Shibata, R., Kai, H., Seki, Y., Kusaba, K., Takemiya, K., Koga, M., Jalalidin, A., Tokuda, K., Tahara, N., Niiyama, H., Nagata, T., Kuwahara, F., Imaizumi, T. J. Cardiovasc. Pharmacol. (2003) [Pubmed]
  32. Myc potentiates apoptosis by stimulating Bax activity at the mitochondria. Soucie, E.L., Annis, M.G., Sedivy, J., Filmus, J., Leber, B., Andrews, D.W., Penn, L.Z. Mol. Cell. Biol. (2001) [Pubmed]
  33. RhoA/Rho kinase up-regulate Bax to activate a mitochondrial death pathway and induce cardiomyocyte apoptosis. Del Re, D.P., Miyamoto, S., Brown, J.H. J. Biol. Chem. (2007) [Pubmed]
  34. Nitric oxide and superoxide induced p53 and Bax accumulation during mesangial cell apoptosis. Sandau, K., Pfeilschifter, J., Brüne, B. Kidney Int. (1997) [Pubmed]
  35. Dynamic changes of the anti- and pro-apoptotic proteins Bcl-w, Bcl-2, and Bax with Smac/Diablo mitochondrial release after photothrombotic ring stroke in rats. Hu, X.L., Olsson, T., Johansson, I.M., Brännström, T., Wester, P. Eur. J. Neurosci. (2004) [Pubmed]
  36. Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. Shan, Y.X., Liu, T.J., Su, H.F., Samsamshariat, A., Mestril, R., Wang, P.H. J. Mol. Cell. Cardiol. (2003) [Pubmed]
  37. Thrombin induces nigral dopaminergic neurodegeneration in vivo by altering expression of death-related proteins. Choi, S.H., Lee, d.a. .Y., Ryu, J.K., Kim, J., Joe, E.H., Jin, B.K. Neurobiol. Dis. (2003) [Pubmed]
  38. Glucose enhances mesangial cell apoptosis. Khera, T., Martin, J., Riley, S., Steadman, R., Phillips, A.O. Lab. Invest. (2006) [Pubmed]
  39. Vasectomy impairs spermatogenesis through germ cell apoptosis mediated by the p53-Bax pathway in rats. Shiraishi, K., Naito, K., Yoshida, K. J. Urol. (2001) [Pubmed]
WikiGenes - Universities