Bcl-2-interacting killer

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BCL2-interacting killer (apoptosis-inducing)
Identifiers
Symbol(s) BIK; BIP1; BP4; NBK
External IDs OMIM: 603392 MGI1206591 HomoloGene924
Orthologs
Human Mouse
Entrez 638 12124
Ensembl ENSG00000100290 ENSMUSG00000016758
Uniprot Q13323 n/a
Refseq NM_001197 (mRNA)
NP_001188 (protein)
XM_001001652 (mRNA)
XP_001001652 (protein)
Location Chr 22: 41.84 - 41.86 Mb Chr 15: 83.35 - 83.37 Mb
Pubmed search [1] [2]

BCL2-interacting killer (apoptosis-inducing), also known as BIK, is a human gene.[1]

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 programed 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.[1]

[edit] References

[edit] Further reading

  • Boyd JM, Gallo GJ, Elangovan B, et al. (1995). "Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins.". Oncogene 11 (9): 1921–8. PMID 7478623. 
  • Chittenden T, Flemington C, Houghton AB, et al. (1996). "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions.". EMBO J. 14 (22): 5589–96. PMID 8521816. 
  • Han J, Sabbatini P, White E (1996). "Induction of apoptosis by human Nbk/Bik, a BH3-containing protein that interacts with E1B 19K.". Mol. Cell. Biol. 16 (10): 5857–64. PMID 8816500. 
  • Inohara N, Ding L, Chen S, Núñez G (1997). "harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L).". EMBO J. 16 (7): 1686–94. doi:10.1093/emboj/16.7.1686. PMID 9130713. 
  • Huang DC, Adams JM, Cory S (1998). "The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4.". EMBO J. 17 (4): 1029–39. doi:10.1093/emboj/17.4.1029. PMID 9463381. 
  • Hegde R, Srinivasula SM, Ahmad M, et al. (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. PMID 9525867. 
  • Ohi N, Tokunaga A, Tsunoda H, et al. (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. PMID 10381623. 
  • 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. PMID 10381646. 
  • Castells A, Ino Y, Louis DN, et al. (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. PMID 10500065. 
  • Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208. 
  • 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. PMID 10974546. 
  • 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. PMID 11342619. 
  • Federici M, Hribal M, Perego L, et al. (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. PMID 11375329. 
  • Zou Y, Peng H, Zhou B, et al. (2002). "Systemic tumor suppression by the proapoptotic gene bik.". Cancer Res. 62 (1): 8–12. PMID 11782349. 
  • 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. PMID 11884414. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Gillissen B, Essmann F, Graupner V, et al. (2003). "Induction of cell death by the BH3-only Bcl-2 homolog Nbk/Bik is mediated by an entirely Bax-dependent mitochondrial pathway.". EMBO J. 22 (14): 3580–90. doi:10.1093/emboj/cdg343. PMID 12853473. 
  • Arena V, Martini M, Luongo M, et al. (2003). "Mutations of the BIK gene in human peripheral B-cell lymphomas.". Genes Chromosomes Cancer 38 (1): 91–6. doi:10.1002/gcc.10245. PMID 12874789. 
  • Hur J, Chesnes J, Coser KR, et al. (2004). "The Bik BH3-only protein is induced in estrogen-starved and antiestrogen-exposed breast cancer cells and provokes apoptosis.". Proc. Natl. Acad. Sci. U.S.A. 101 (8): 2351–6. PMID 14983013. 
  • Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMID 15461802.