The protein encoded by this gene is known to interact with cellular and viral survival-promoting proteins, such as BCL2 and the Epstein-Barr virus in order to enhance programmed cell death. Because its activity is suppressed in the presence of survival-promoting proteins, this protein is suggested as a likely target for antiapoptotic proteins. This protein shares a critical BH3 domain with other death-promoting proteins, BAX and BAK.[3]
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↑ 5.05.1Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC (February 2005). "Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function". Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID15694340.
↑Jiang A, Clark EA (May 2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. 166 (10): 6025–33. doi:10.4049/jimmunol.166.10.6025. PMID11342619.
Hegde R, Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES (1998). "Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist". J. Biol. Chem. 273 (14): 7783–6. doi:10.1074/jbc.273.14.7783. PMID9525867.
Ohi N, Tokunaga A, Tsunoda H, Nakano K, Haraguchi K, Oda K, Motoyama N, Nakajima T (1999). "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region". Cell Death Differ. 6 (4): 314–25. doi:10.1038/sj.cdd.4400493. PMID10381623.
Holmgreen SP, Huang DC, Adams JM, Cory S (1999). "Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members". Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID10381646.
Castells A, Ino Y, Louis DN, Ramesh V, Gusella JF, Rustgi AK (1999). "Mapping of a target region of allelic loss to a 0.5-cM interval on chromosome 22q13 in human colorectal cancer". Gastroenterology. 117 (4): 831–7. doi:10.1016/S0016-5085(99)70341-0. PMID10500065.
Verma S, Budarf ML, Emanuel BS, Chinnadurai G (2000). "Structural analysis of the human pro-apoptotic gene Bik: chromosomal localization, genomic organization and localization of promoter sequences". Gene. 254 (1–2): 157–62. doi:10.1016/S0378-1119(00)00276-6. PMID10974546.
Jiang A, Clark EA (2001). "Involvement of Bik, a proapoptotic member of the Bcl-2 family, in surface IgM-mediated B cell apoptosis". J. Immunol. 166 (10): 6025–33. doi:10.4049/jimmunol.166.10.6025. PMID11342619.
Federici M, Hribal M, Perego L, Ranalli M, Caradonna Z, Perego C, Usellini L, Nano R, Bonini P, Bertuzzi F, Marlier LN, Davalli AM, Carandente O, Pontiroli AE, Melino G, Marchetti P, Lauro R, Sesti G, Folli F (2001). "High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: a potential role for regulation of specific Bcl family genes toward an apoptotic cell death program". Diabetes. 50 (6): 1290–301. doi:10.2337/diabetes.50.6.1290. PMID11375329.
Zou Y, Peng H, Zhou B, Wen Y, Wang SC, Tsai EM, Hung MC (2002). "Systemic tumor suppression by the proapoptotic gene bik". Cancer Res. 62 (1): 8–12. PMID11782349.
Germain M, Mathai JP, Shore GC (2002). "BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria". J. Biol. Chem. 277 (20): 18053–60. doi:10.1074/jbc.M201235200. PMID11884414.
Arena V, Martini M, Luongo M, Capelli A, Larocca LM (2003). "Mutations of the BIK gene in human peripheral B-cell lymphomas". Genes Chromosomes Cancer. 38 (1): 91–6. doi:10.1002/gcc.10245. PMID12874789.