Caspase-9

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Caspase 9, apoptosis-related cysteine peptidase
PDB rendering based on 1jxq.
Available structures: 1jxq, 1nw9, 2ar9, 3ygs
Identifiers
Symbol(s) CASP9; APAF-3; APAF3; CASPASE-9c; ICE-LAP6; MCH6
External IDs OMIM: 602234 MGI: 1277950 HomoloGene: 31024
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 842 12371
Ensembl ENSG00000132906 ENSMUSG00000028914
Uniprot P55211 n/a
Refseq NM_001229 (mRNA)
NP_001220 (protein)		 NM_015733 (mRNA)
NP_056548 (protein)
Location Chr 1: 15.69 - 15.72 Mb Chr 4: 141.07 - 141.09 Mb
Pubmed search [1] [2]

Caspase-9 is an initiator caspase.[1]

The aspartic acid specific protease caspase-9 has been linked to the mitochondrial death pathway. It is activated during programmed cell death (apoptosis). Induction of stress signalling pathways JNK/SAPK causes release of cytochrome c from mitochondria and activation of apaf-1 (apoptosome), which in turn cleaves the pro-enzyme of caspase-9 into the active form.

Once intiated caspase-9 goes on to cleave procaspase-3 & procaspase-7 and which cleave several cellular targets, including poly ADP ribose polymerase.

[edit] References

  1. ^ Caspase 9

[edit] External links

  • Lei K, Nimnual A, Zong W, Kennedy N, Flavell R, Thompson C, Bar-Sagi D, Davis R (2002). "The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinase.". Mol Cell Biol 22 (13): 4929–42. doi:10.1128/MCB.22.13.4929-4942.2002. PMID 12052897. 
  • Earnshaw W, Martins L, Kaufmann S. "Mammalian caspases: structure, activation, substrates, and functions during apoptosis.". Annu Rev Biochem 68: 383–424. doi:10.1146/annurev.biochem.68.1.383. PMID 10872455. 

[edit] Further reading

  • Cohen GM (1997). "Caspases: the executioners of apoptosis.". Biochem. J. 326 ( Pt 1): 1–16. PMID 9337844. 
  • Deveraux QL, Reed JC (1999). "IAP family proteins--suppressors of apoptosis.". Genes Dev. 13 (3): 239–52. PMID 9990849. 
  • Zhao LJ, Zhu H (2005). "Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design.". Curr. Drug Targets Immune Endocr. Metabol. Disord. 4 (4): 265–75. PMID 15578977. 
  • Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle.". Retrovirology 2: 11. doi:10.1186/1742-4690-2-11. PMID 15725353. 
  • Moon HS, Yang JS (2006). "Role of HIV Vpr as a regulator of apoptosis and an effector on bystander cells.". Mol. Cells 21 (1): 7–20. PMID 16511342. 
  • Kopp S (1976). "Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction.". Community dentistry and oral epidemiology 4 (5): 205–9. PMID 1067155. 
  • Fernandes-Alnemri T, Litwack G, Alnemri ES (1995). "CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme.". J. Biol. Chem. 269 (49): 30761–4. PMID 7983002. 
  • Duan H, Orth K, Chinnaiyan AM, et al. (1996). "ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B.". J. Biol. Chem. 271 (28): 16720–4. PMID 8663294. 
  • Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, et al. (1996). "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32.". J. Biol. Chem. 271 (43): 27099–106. PMID 8900201. 
  • Srinivasula SM, Ahmad M, Fernandes-Alnemri T, et al. (1997). "Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases.". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. PMID 8962078. 
  • Kothakota S, Azuma T, Reinhard C, et al. (1997). "Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis.". Science 278 (5336): 294–8. PMID 9323209. 
  • Li P, Nijhawan D, Budihardjo I, et al. (1997). "Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.". Cell 91 (4): 479–89. PMID 9390557. 
  • Pan G, O'Rourke K, Dixit VM (1998). "Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex.". J. Biol. Chem. 273 (10): 5841–5. PMID 9488720. 
  • Hu Y, Benedict MA, Wu D, et al. (1998). "Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation.". Proc. Natl. Acad. Sci. U.S.A. 95 (8): 4386–91. PMID 9539746. 
  • Deveraux QL, Roy N, Stennicke HR, et al. (1998). "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases.". EMBO J. 17 (8): 2215–23. doi:10.1093/emboj/17.8.2215. PMID 9545235. 
  • Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES (1998). "Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization.". Mol. Cell 1 (7): 949–57. PMID 9651578. 
  • Kamada S, Kusano H, Fujita H, et al. (1998). "A cloning method for caspase substrates that uses the yeast two-hybrid system: cloning of the antiapoptotic gene gelsolin.". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8532–7. PMID 9671712. 
  • Cardone MH, Roy N, Stennicke HR, et al. (1998). "Regulation of cell death protease caspase-9 by phosphorylation.". Science 282 (5392): 1318–21. PMID 9812896. 
  • Hu Y, Ding L, Spencer DM, Núñez G (1999). "WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation.". J. Biol. Chem. 273 (50): 33489–94. PMID 9837928. 
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