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Gene Review

CASP9  -  caspase 9, apoptosis-related cysteine...

Homo sapiens

Synonyms: APAF-3, APAF3, Apoptotic protease Mch-6, Apoptotic protease-activating factor 3, CASP-9, ...
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Disease relevance of CASP9


High impact information on CASP9

  • The majority of Casp9 knockout mice die perinatally with a markedly enlarged and malformed cerebrum caused by reduced apoptosis during brain development [5].
  • Cytochrome c-induced proteolytic processing of pro-Casp9 was defective in cytosolic extracts from cells expressing either active Ras or Akt [6].
  • The kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells [6].
  • Finally, several genes in this pathway, including APAF1, CASP9 and CASP3, have been shown to be associated with dramatic defects in neuronal cell number and brain size when mutated in mice [7].
  • Caspase-9 (CASP-9) is an initiator CASP in the apoptosome-driven apoptosis pathway and plays an important role in the development and progression of cancer [3].

Biological context of CASP9


Anatomical context of CASP9


Associations of CASP9 with chemical compounds


Physical interactions of CASP9

  • Molecular modeling supports the conclusion that Arg(10) in the D domain of caspase-9 interacts with Asp(160) in the TTCD motif of ERK2 [11].

Enzymatic interactions of CASP9

  • We demonstrate that the pro-enzymes of Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for mature CPP32 [12].

Regulatory relationships of CASP9

  • These data suggest that Mch2alpha and Mch6 are downstream proteases activated in CPP32- and granzyme B-mediated apoptosis [12].
  • Mutational analysis revealed that only a small portion of the CED-4 homologous region (residues 456-559) could be deleted without destroying the ability of Apaf-1-(1-559) to activate pro-casp9 [13].

Other interactions of CASP9


  1. Analyses of apoptotic regulators CASP9 and DFFA at 1P36.2, reveal rare allele variants in human neuroblastoma tumours. Abel, F., Sjöberg, R.M., Ejeskär, K., Krona, C., Martinsson, T. Br. J. Cancer (2002) [Pubmed]
  2. Caspase-9 and Apaf-1 are expressed and functionally active in human neuroblastoma tumor cell lines with 1p36 LOH and amplified MYCN. Teitz, T., Wei, T., Liu, D., Valentine, V., Valentine, M., Grenet, J., Lahti, J.M., Kidd, V.J. Oncogene (2002) [Pubmed]
  3. Caspase 9 promoter polymorphisms and risk of primary lung cancer. Park, J.Y., Park, J.M., Jang, J.S., Choi, J.E., Kim, K.M., Cha, S.I., Kim, C.H., Kang, Y.M., Lee, W.K., Kam, S., Park, R.W., Kim, I.S., Lee, J.T., Jung, T.H. Hum. Mol. Genet. (2006) [Pubmed]
  4. Inhibition of caspase-9 activity and Apaf-1 expression in cisplatin-resistant head and neck squamous cell carcinoma cells. Kuwahara, D., Tsutsumi, K., Oyake, D., Ohta, T., Nishikawa, H., Koizuka, I. Auris, nasus, larynx. (2003) [Pubmed]
  5. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Kuida, K., Haydar, T.F., Kuan, C.Y., Gu, Y., Taya, C., Karasuyama, H., Su, M.S., Rakic, P., Flavell, R.A. Cell (1998) [Pubmed]
  6. Regulation of cell death protease caspase-9 by phosphorylation. Cardone, M.H., Roy, N., Stennicke, H.R., Salvesen, G.S., Franke, T.F., Stanbridge, E., Frisch, S., Reed, J.C. Science (1998) [Pubmed]
  7. A primate-specific acceleration in the evolution of the caspase-dependent apoptosis pathway. Vallender, E.J., Lahn, B.T. Hum. Mol. Genet. (2006) [Pubmed]
  8. ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. Duan, H., Orth, K., Chinnaiyan, A.M., Poirier, G.G., Froelich, C.J., He, W.W., Dixit, V.M. J. Biol. Chem. (1996) [Pubmed]
  9. Two novel single-nucleotide polymorphisms of the Caspase-9 (CASP9) gene in the Japanese population. Hirano, A., Nagai, H., Harada, H., Haga, S., Kajiwara, T., Emi, M. Genes Immun. (2001) [Pubmed]
  10. Caspase-9 regulates cisplatin-induced apoptosis in human head and neck squamous cell carcinoma cells. Kuwahara, D., Tsutsumi, K., Kobayashi, T., Hasunuma, T., Nishioka, K. Cancer Lett. (2000) [Pubmed]
  11. The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125. Martin, M.C., Allan, L.A., Mancini, E.J., Clarke, P.R. J. Biol. Chem. (2008) [Pubmed]
  12. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. Srinivasula, S.M., Fernandes-Alnemri, T., Zangrilli, J., Robertson, N., Armstrong, R.C., Wang, L., Trapani, J.A., Tomaselli, K.J., Litwack, G., Alnemri, E.S. J. Biol. Chem. (1996) [Pubmed]
  13. WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. Hu, Y., Ding, L., Spencer, D.M., Núñez, G. J. Biol. Chem. (1998) [Pubmed]
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