Baculoviral IAP repeat-containing protein3 (also known as cIAP2) is a protein that in humans is encoded by the BIRC3gene.[1][2]
cIAP2 is a member of the inhibitor of apoptosis family that inhibit apoptosis by interfering with the activation of caspases. The encoded protein inhibits apoptosis induced by serum deprivation but does not affect apoptosis resulting from exposure to menadione, a potent inducer of free radicals. The cIAP2 protein contains three BIR domains, a UBA domain, a CARD domain and a RING finger domain. Transcript variants encoding the same isoform have been identified.[3]
↑Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G, Farahani R, McLean M, Ikeda JE, MacKenzie A, Korneluk RG (February 1996). "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes". Nature. 379 (6563): 349–53. doi:10.1038/379349a0. PMID8552191.
↑Rothe M, Pan MG, Henzel WJ, Ayres TM, Goeddel DV (February 1996). "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins". Cell. 83 (7): 1243–52. doi:10.1016/0092-8674(95)90149-3. PMID8548810.
↑Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, Gillard JW, Jaquith JB, Morris SJ, Barker PA (2008). "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell. 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID18570872.
↑ 7.07.1Li X, Yang Y, Ashwell JD (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature. 416 (6878): 345–7. doi:10.1038/416345a. PMID11907583.
↑Yoneda T, Imaizumi K, Maeda M, Yui D, Manabe T, Katayama T, Sato N, Gomi F, Morihara T, Mori Y, Miyoshi K, Hitomi J, Ugawa S, Yamada S, Okabe M, Tohyama M (2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–20. doi:10.1074/jbc.275.15.11114. PMID10753917.
↑Mace PD, Linke K, Feltham R, Schumacher FR, Smith CA, Vaux DL, Silke J, Day CL (2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem. 283 (46): 31633–40. doi:10.1074/jbc.M804753200. PMID18784070.
Further reading
Bertoni F, Cavalli F, Cotter FE, Zucca E (2003). "Genetic alterations underlying the pathogenesis of MALT lymphoma". Hematol. J. 3 (1): 10–3. doi:10.1038/sj.thj.6200146. PMID11960389.
Rajcan-Separovic E, Liston P, Lefebvre C, Korneluk RG (1997). "Assignment of human inhibitor of apoptosis protein (IAP) genes xiap, hiap-1, and hiap-2 to chromosomes Xq25 and 11q22-q23 by fluorescence in situ hybridization". Genomics. 37 (3): 404–6. doi:10.1006/geno.1996.0579. PMID8938457.
Young SS, Liston P, Xuan JY, et al. (1999). "Genomic organization and physical map of the human inhibitors of apoptosis: HIAP1 and HIAP2". Mamm. Genome. 10 (1): 44–8. doi:10.1007/s003359900940. PMID9892732.
Horrevoets AJ, Fontijn RD, van Zonneveld AJ, et al. (1999). "Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes". Blood. 93 (10): 3418–31. PMID10233894.
Suzuki H, Motegi M, Akagi T, et al. (1999). "API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18)(q21;q21)". Blood. 94 (9): 3270–1. PMID10610122.
Huang H, Joazeiro CA, Bonfoco E, et al. (2000). "The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7". J. Biol. Chem. 275 (35): 26661–4. doi:10.1074/jbc.C000199200. PMID10862606.
Verhagen AM, Ekert PG, Pakusch M, et al. (2000). "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins". Cell. 102 (1): 43–53. doi:10.1016/S0092-8674(00)00009-X. PMID10929712.
Baens M, Steyls A, Dierlamm J, et al. (2001). "Structure of the MLT gene and molecular characterization of the genomic breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell lymphomas of MALT type". Genes Chromosomes Cancer. 29 (4): 281–91. doi:10.1002/1098-2264(2000)9999:9999<::AID-GCC1036>3.0.CO;2-I. PMID11066071.
Werneburg BG, Zoog SJ, Dang TT, et al. (2001). "Molecular characterization of CD40 signaling intermediates". J. Biol. Chem. 276 (46): 43334–42. doi:10.1074/jbc.M104994200. PMID11562359.
Suzuki Y, Imai Y, Nakayama H, et al. (2001). "A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death". Mol. Cell. 8 (3): 613–21. doi:10.1016/S1097-2765(01)00341-0. PMID11583623.
Li X, Yang Y, Ashwell JD (2002). "TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2". Nature. 416 (6878): 345–7. doi:10.1038/416345a. PMID11907583.
Gordon GJ, Appasani K, Parcells JP, et al. (2002). "Inhibitor of apoptosis protein-1 promotes tumor cell survival in mesothelioma". Carcinogenesis. 23 (6): 1017–24. doi:10.1093/carcin/23.6.1017. PMID12082024.
Sharief MK, Noori MA, Zoukos Y (2002). "Reduced expression of the inhibitor of apoptosis proteins in T cells from patients with multiple sclerosis following interferon-beta therapy". J. Neuroimmunol. 129 (1–2): 224–31. doi:10.1016/S0165-5728(02)00185-6. PMID12161039.
Ekedahl J, Joseph B, Grigoriev MY, et al. (2002). "Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells". Exp. Cell Res. 279 (2): 277–90. doi:10.1006/excr.2002.5608. PMID12243753.