BAK1

From Wikipedia, the free encyclopedia

BCL2-antagonist/killer 1

PDB rendering based on 2ims.

Available structures: 2ims, 2imt, 2jcn

Identifiers

Symbol(s)

BAK1; BAK; BAK-LIKE; BCL2L7; CDN1; MGC117255; MGC3887

External IDs

OMIM: 600516 MGI: 1097161 HomoloGene: 917

Gene ontology
Molecular Function:	• identical protein binding • protein heterodimerization activity
Cellular Component:	• membrane • integral to membrane
Biological Process:	• induction of apoptosis • apoptotic mitochondrial changes • regulation of apoptosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001188 (mRNA)
NP_001179 (protein)

NM_007523 (mRNA)
NP_031549 (protein)

Location

Chr 6: 33.65 - 33.66 Mb

Chr 17: 26.75 - 26.76 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ Entrez Gene: BAK1 BCL2-antagonist/killer 1.

[edit] Further reading

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.