BAK1

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

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: BAK1 BCL2-antagonist/killer 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=578| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Buytaert E, Callewaert G, Vandenheede JR, Agostinis P |title=Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum. |journal=Autophagy |volume=2 |issue= 3 |pages= 238–40 |year= 2007 |pmid= 16874066 |doi=
*cite journal | author=Farrow SN, White JH, Martinou I, "et al." |title=Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K. |journal=Nature |volume=374 |issue= 6524 |pages= 731–3 |year= 1995 |pmid= 7715729 |doi= 10.1038/374731a0
*cite journal | author=Chittenden T, Harrington EA, O'Connor R, "et al." |title=Induction of apoptosis by the Bcl-2 homologue Bak. |journal=Nature |volume=374 |issue= 6524 |pages= 733–6 |year= 1995 |pmid= 7715730 |doi= 10.1038/374733a0
*cite journal | author=Kiefer MC, Brauer MJ, Powers VC, "et al." |title=Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. |journal=Nature |volume=374 |issue= 6524 |pages= 736–9 |year= 1995 |pmid= 7715731 |doi= 10.1038/374736a0
*cite journal | author=Chittenden T, Flemington C, Houghton AB, "et al." |title=A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5589–96 |year= 1996 |pmid= 8521816 |doi=
*cite journal | author=Sattler M, Liang H, Nettesheim D, "et al." |title=Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. |journal=Science |volume=275 |issue= 5302 |pages= 983–6 |year= 1997 |pmid= 9020082 |doi=
*cite journal | author=Diaz JL, Oltersdorf T, Horne W, "et al." |title=A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11350–5 |year= 1997 |pmid= 9111042 |doi=
*cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029–39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029
*cite journal | author=Herberg JA, Phillips S, Beck S, "et al." |title=Genomic structure and domain organisation of the human Bak gene. |journal=Gene |volume=211 |issue= 1 |pages= 87–94 |year= 1998 |pmid= 9573342 |doi=
*cite journal | author=Narita M, Shimizu S, Ito T, "et al." |title=Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 25 |pages= 14681–6 |year= 1999 |pmid= 9843949 |doi=
*cite journal | author=Song Q, Kuang Y, Dixit VM, Vincenz C |title=Boo, a novel negative regulator of cell death, interacts with Apaf-1. |journal=EMBO J. |volume=18 |issue= 1 |pages= 167–78 |year= 1999 |pmid= 9878060 |doi= 10.1093/emboj/18.1.167
*cite journal | author=Griffiths GJ, Dubrez L, Morgan CP, "et al." |title=Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. |journal=J. Cell Biol. |volume=144 |issue= 5 |pages= 903–14 |year= 1999 |pmid= 10085290 |doi=
*cite journal | author=Shimizu S, Narita M, Tsujimoto Y |title=Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. |journal=Nature |volume=399 |issue= 6735 |pages= 483–7 |year= 1999 |pmid= 10365962 |doi= 10.1038/20959
*cite journal | author=Ohi N, Tokunaga A, Tsunoda H, "et al." |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314–25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493
*cite journal | author=Holmgreen SP, Huang DC, Adams JM, Cory S |title=Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members. |journal=Cell Death Differ. |volume=6 |issue= 6 |pages= 525–32 |year= 1999 |pmid= 10381646 |doi= 10.1038/sj.cdd.4400519
*cite journal | author=Leo CP, Hsu SY, Chun SY, "et al." |title=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. |journal=Endocrinology |volume=140 |issue= 12 |pages= 5469–77 |year= 1999 |pmid= 10579309 |doi=
*cite journal | author=Shimizu S, Tsujimoto Y |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 577–82 |year= 2000 |pmid= 10639121 |doi=
*cite journal | author=Bae J, Leo CP, Hsu SY, Hsueh AJ |title=MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25255–61 |year= 2000 |pmid= 10837489 |doi= 10.1074/jbc.M909826199
*cite journal | author=Wei MC, Lindsten T, Mootha VK, "et al." |title=tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. |journal=Genes Dev. |volume=14 |issue= 16 |pages= 2060–71 |year= 2000 |pmid= 10950869 |doi=
*cite journal | author=Degterev A, Lugovskoy A, Cardone M, "et al." |title=Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL. |journal=Nat. Cell Biol. |volume=3 |issue= 2 |pages= 173–82 |year= 2001 |pmid= 11175750 |doi=

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