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BAK1

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BCL2-antagonist/killer 1
PDB rendering based on 2ims.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols BAK1 ; BAK; BAK-LIKE; BCL2L7; CDN1; MGC117255; MGC3887
External IDs Template:OMIM5 Template:MGI HomoloGene: 917
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

BCL2-antagonist/killer 1, also known as BAK1, is a human gene.

The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.[1]

References[edit | edit source]

  1. ↑ "Entrez Gene: BAK1 BCL2-antagonist/killer 1".

Further reading[edit | edit source]

  • Buytaert E, Callewaert G, Vandenheede JR, Agostinis P (2007). "Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum". Autophagy. 2 (3): 238–40. PMID 16874066.
  • Farrow SN, White JH, Martinou I; et al. (1995). "Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K". Nature. 374 (6524): 731–3. doi:10.1038/374731a0. PMID 7715729.
  • Chittenden T, Harrington EA, O'Connor R; et al. (1995). "Induction of apoptosis by the Bcl-2 homologue Bak". Nature. 374 (6524): 733–6. doi:10.1038/374733a0. PMID 7715730.
  • Kiefer MC, Brauer MJ, Powers VC; et al. (1995). "Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak". Nature. 374 (6524): 736–9. doi:10.1038/374736a0. PMID 7715731.
  • 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.
  • Sattler M, Liang H, Nettesheim D; et al. (1997). "Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis". Science. 275 (5302): 983–6. PMID 9020082.
  • Diaz JL, Oltersdorf T, Horne W; et al. (1997). "A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members". J. Biol. Chem. 272 (17): 11350–5. PMID 9111042.
  • 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.
  • Herberg JA, Phillips S, Beck S; et al. (1998). "Genomic structure and domain organisation of the human Bak gene". Gene. 211 (1): 87–94. PMID 9573342.
  • Narita M, Shimizu S, Ito T; et al. (1999). "Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14681–6. PMID 9843949.
  • Song Q, Kuang Y, Dixit VM, Vincenz C (1999). "Boo, a novel negative regulator of cell death, interacts with Apaf-1". EMBO J. 18 (1): 167–78. doi:10.1093/emboj/18.1.167. PMID 9878060.
  • Griffiths GJ, Dubrez L, Morgan CP; et al. (1999). "Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis". J. Cell Biol. 144 (5): 903–14. PMID 10085290.
  • Shimizu S, Narita M, Tsujimoto Y (1999). "Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC". Nature. 399 (6735): 483–7. doi:10.1038/20959. PMID 10365962.
  • 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.
  • Leo CP, Hsu SY, Chun SY; et al. (1999). "Characterization of the antiapoptotic Bcl-2 family member myeloid cell leukemia-1 (Mcl-1) and the stimulation of its message by gonadotropins in the rat ovary". Endocrinology. 140 (12): 5469–77. PMID 10579309.
  • Shimizu S, Tsujimoto Y (2000). "Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 577–82. PMID 10639121.
  • Bae J, Leo CP, Hsu SY, Hsueh AJ (2000). "MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain". J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.
  • Wei MC, Lindsten T, Mootha VK; et al. (2000). "tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.". Genes Dev. 14 (16): 2060–71. PMID 10950869.
  • Degterev A, Lugovskoy A, Cardone M; et al. (2001). "Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL". Nat. Cell Biol. 3 (2): 173–82. PMID 11175750.

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