Caspase 6
From Wikipedia, the free encyclopedia
Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene.[1][2] CASP6 orthologs [3] have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family.[4] Alternative splicing of this gene results in two transcript variants that encode different isoforms.[5]
Interactions
Caspase 6 has been shown to interact with Caspase 8.[6][7][8]
References
- ↑ Tiso N, Pallavicini A, Muraro T, Zimbello R, Apolloni E, Valle G, Lanfranchi G, Danieli GA (Oct 1996). "Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis". Biochem Biophys Res Commun 225 (3): 983–9. doi:10.1006/bbrc.1996.1282. PMID 8780721.
- ↑ Fernandes-Alnemri T, Litwack G, Alnemri ES (Aug 1995). "Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family". Cancer Res 55 (13): 2737–42. PMID 7796396.
- ↑ "OrthoMaM phylogenetic marker: CASP6 coding sequence".
- ↑ Wang XJ, Cao Q, Liu X, Wang KT, Mi W, Zhang Y, Li LF, LeBlanc AC, Su XD (Nov 2010). "Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation". EMBO Rep 11 (11): 841–7. doi:10.1038/embor.2010.141. PMC 2966951. PMID 20890311.
- ↑ "Entrez Gene: CASP6 caspase 6, apoptosis-related cysteine peptidase".
- ↑ Cowling, V; Downward J (Oct 2002). "Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain". Cell Death Differ. (England) 9 (10): 1046–56. doi:10.1038/sj.cdd.4401065. ISSN 1350-9047. PMID 12232792.
- ↑ Guo, Yin; Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (Apr 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. (United States) 277 (16): 13430–7. doi:10.1074/jbc.M108029200. ISSN 0021-9258. PMID 11832478.
- ↑ Srinivasula, S M; Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri E S (Dec 1996). "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. (UNITED STATES) 93 (25): 14486–91. doi:10.1073/pnas.93.25.14486. ISSN 0027-8424. PMC 26159. PMID 8962078.
External links
See also
Further reading
- Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 ( Pt 1) (Pt 1): 1–16. PMC 1218630. PMID 9337844.
- 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.
- Takahashi A, Alnemri ES, Lazebnik YA et al. (1996). "Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis". Proc. Natl. Acad. Sci. U.S.A. 93 (16): 8395–400. doi:10.1073/pnas.93.16.8395. PMC 38682. PMID 8710882.
- Bullrich F, Fernandes-Alnemri T, Litwack G et al. (1997). "Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3". Genomics 36 (2): 362–5. doi:10.1006/geno.1996.0476. PMID 8812467.
- 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. doi:10.1074/jbc.271.43.27099. 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. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
- Rao L, Perez D, White E (1997). "Lamin proteolysis facilitates nuclear events during apoptosis". J. Cell Biol. 135 (6 Pt 1): 1441–55. doi:10.1083/jcb.135.6.1441. PMC 2133948. PMID 8978814.
- Kim TW, Pettingell WH, Jung YK et al. (1998). "Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease". Science 277 (5324): 373–6. doi:10.1126/science.277.5324.373. PMID 9219695.
- Srinivasula SM, Ahmad M, Ottilie S et al. (1997). "FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis". J. Biol. Chem. 272 (30): 18542–5. doi:10.1074/jbc.272.30.18542. PMID 9228018.
- Caulín C, Salvesen GS, Oshima RG (1997). "Caspase Cleavage of Keratin 18 and Reorganization of Intermediate Filaments during Epithelial Cell Apoptosis". J. Cell Biol. 138 (6): 1379–94. doi:10.1083/jcb.138.6.1379. PMC 2132555. PMID 9298992.
- Hirata H, Takahashi A, Kobayashi S et al. (1998). "Caspases Are Activated in a Branched Protease Cascade and Control Distinct Downstream Processes in Fas-induced Apoptosis". J. Exp. Med. 187 (4): 587–600. doi:10.1084/jem.187.4.587. PMC 2212161. PMID 9463409.
- Harvey KF, Harvey NL, Michael JM et al. (1998). "Caspase-mediated cleavage of the ubiquitin-protein ligase Nedd4 during apoptosis". J. Biol. Chem. 273 (22): 13524–30. doi:10.1074/jbc.273.22.13524. PMID 9593687.
- Utz PJ, Hottelet M, Le TM et al. (1999). "The 72-kDa component of signal recognition particle is cleaved during apoptosis". J. Biol. Chem. 273 (52): 35362–70. doi:10.1074/jbc.273.52.35362. PMID 9857079.
- Samejima K, Svingen PA, Basi GS et al. (1999). "Caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis". J. Biol. Chem. 274 (7): 4335–40. doi:10.1074/jbc.274.7.4335. PMID 9933635.
- Walter J, Schindzielorz A, Grünberg J, Haass C (1999). "Phosphorylation of presenilin-2 regulates its cleavage by caspases and retards progression of apoptosis". Proc. Natl. Acad. Sci. U.S.A. 96 (4): 1391–6. doi:10.1073/pnas.96.4.1391. PMC 15473. PMID 9990034.
- van de Craen M (1999). "Identification of caspases that cleave presenilin-1 and presenilin-2. Five presenilin-1 (PS1) mutations do not alter the sensitivity of PS1 to caspases". FEBS Lett. 445 (1): 149–54. doi:10.1016/S0014-5793(99)00108-8. PMID 10069390.
- Xanthoudakis S, Roy S, Rasper D et al. (1999). "Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis". EMBO J. 18 (8): 2049–56. doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
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