Caspase 10

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Template:Cs1 config Template:Short description An Error has occurred retrieving Wikidata item for infobox Caspase-10 is an enzyme that, in humans, is encoded by the CASP10 gene.[1]

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.

That protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in this gene are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.[2]

Interactions

Caspase 10 has been shown to interact with FADD,[3][4][5] CFLAR,[4][6][7] Caspase 8,[8][9][10] Fas receptor,[8][3][11] RYBP,[12] TNFRSF1A[8][3] and TNFRSF10B.[8][11]

See also

References

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  1. ^ Page Module:Citation/CS1/styles.css has no content.Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES (October 1996). "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains". Proc Natl Acad Sci USA. 93 (15): 7464–9. Bibcode:1996PNAS...93.7464F. doi:10.1073/pnas.93.15.7464. PMC 38767. PMID 8755496.
  2. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: CASP10 caspase 10, apoptosis-related cysteine peptidase".
  3. ^ a b c Page Module:Citation/CS1/styles.css has no content.Vincenz C, Dixit V M (March 1997). "Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling". J. Biol. Chem. 272 (10). UNITED STATES: 6578–83. doi:10.1074/jbc.272.10.6578. ISSN 0021-9258. PMID 9045686.
  4. ^ a b Page Module:Citation/CS1/styles.css has no content.Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES (July 1997). "FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis". J. Biol. Chem. 272 (30). UNITED STATES: 18542–5. doi:10.1074/jbc.272.30.18542. ISSN 0021-9258. PMID 9228018.
  5. ^ Page Module:Citation/CS1/styles.css has no content.Wang J, Chun H J, Wong W, Spencer D M, Lenardo M J (November 2001). "Caspase-10 is an initiator caspase in death receptor signaling". Proc. Natl. Acad. Sci. U.S.A. 98 (24). United States: 13884–8. Bibcode:2001PNAS...9813884W. doi:10.1073/pnas.241358198. ISSN 0027-8424. PMC 61136. PMID 11717445.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Micheau O, Tschopp Jürg (July 2003). "Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes". Cell. 114 (2). United States: 181–90. Bibcode:2003Cell..114..181M. doi:10.1016/S0092-8674(03)00521-X. ISSN 0092-8674. PMID 12887920.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Goltsev YV, Kovalenko A V, Arnold E, Varfolomeev E E, Brodianskii V M, Wallach D (August 1997). "CASH, a novel caspase homologue with death effector domains". J. Biol. Chem. 272 (32). UNITED STATES: 19641–4. doi:10.1074/jbc.272.32.19641. ISSN 0021-9258. PMID 9289491.
  8. ^ a b c d Page Module:Citation/CS1/styles.css has no content.Gajate C, Mollinedo Faustino (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12). United States: 11641–7. doi:10.1074/jbc.M411781200. ISSN 0021-9258. PMID 15659383.
  9. ^ Page Module:Citation/CS1/styles.css has no content.Guo Y, Srinivasula Srinivasa M, Druilhe Anne, Fernandes-Alnemri Teresa, Alnemri Emad S (April 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. 277 (16). United States: 13430–7. doi:10.1074/jbc.M108029200. ISSN 0021-9258. PMID 11832478.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri E S (December 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. 93 (25). UNITED STATES: 14486–91. Bibcode:1996PNAS...9314486S. doi:10.1073/pnas.93.25.14486. ISSN 0027-8424. PMC 26159. PMID 8962078.
  11. ^ a b Page Module:Citation/CS1/styles.css has no content.MacFarlane M, Ahmad M, Srinivasula S M, Fernandes-Alnemri T, Cohen G M, Alnemri E S (October 1997). "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL". J. Biol. Chem. 272 (41). UNITED STATES: 25417–20. doi:10.1074/jbc.272.41.25417. hdl:2381/25106. ISSN 0021-9258. PMID 9325248.
  12. ^ Page Module:Citation/CS1/styles.css has no content.Zheng L, Schickling O, Peter M E, Lenardo M J (August 2001). "The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm". J. Biol. Chem. 276 (34). United States: 31945–52. doi:10.1074/jbc.M102799200. ISSN 0021-9258. PMID 11395500.

Further reading

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