Bak
Bak(Bcl-2 homologous antagonist/killer)またはBAK1(BCL2 antagonist/killer 1)は、ヒトでは6
構造
[BAK1はアポトーシス
機能
[BAK1はBcl-2
臨床 的 意義
[相互 作用
[BAK1は
- BCL2[18][19]
- BCL2L1[20][21][22][23][24]
- MCL1[8][23][25][26][27]
- P53[25]
- Casp8p41[14]
- VDAC2[8]
- MTX2[8]
- BID[10]
- BIM[10]
- PUMA[10]
出典
[- ^ a b c GRCh38: Ensembl release 89: ENSG00000030110 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ “Induction of apoptosis by the Bcl-2 homologue Bak”. Nature 374 (6524): 733–6. (April 1995). Bibcode: 1995Natur.374..733C. doi:10.1038/374733a0. PMID 7715730.
- ^ “Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak”. Nature 374 (6524): 736–9. (April 1995). Bibcode: 1995Natur.374..736K. doi:10.1038/374736a0. PMID 7715731.
- ^ a b c “Entrez Gene: BAK1 BCL2-antagonist/killer 1”. 2021
年 9月 27日 閲覧 。 - ^ a b “Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis”. Cell Death and Differentiation 21 (2): 196–205. (February 2014). doi:10.1038/cdd.2013.139. PMC 3890949. PMID 24162660 .
- ^ a b c d e “Metaxins 1 and 2, two proteins of the mitochondrial protein sorting and assembly machinery, are essential for Bak activation during TNF alpha triggered apoptosis”. Cellular Signalling 26 (9): 1928–34. (September 2014). doi:10.1016/j.cellsig.2014.04.021. PMID 24794530.
- ^ “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. (2006). doi:10.4161/auto.2730. PMID 16874066.
- ^ a b c d “Bioactive lipids and the control of Bax pro-apoptotic activity”. Cell Death & Disease 5 (5): e1266. (May 2014). doi:10.1038/cddis.2014.226. PMC 4047880. PMID 24874738 .
- ^ “BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis”. Science 359 (6378): eaao6047. (February 2018). doi:10.1126/science.aao6047. PMID 29472455.
- ^ “BAK overexpression mediates p53-independent apoptosis inducing effects on human gastric cancer cells”. BMC Cancer 4: 33. (July 2004). doi:10.1186/1471-2407-4-33. PMC 481072. PMID 15248898 .
- ^ “Suppression of apoptosis, crypt hyperplasia, and altered differentiation in the colonic epithelia of bak-null mice”. Gastroenterology 136 (3): 943–52. (March 2009). doi:10.1053/j.gastro.2008.11.036. PMID 19185578.
- ^ a b “Casp8p41 generated by HIV protease kills CD4 T cells through direct Bak activation”. The Journal of Cell Biology 206 (7): 867–76. (September 2014). doi:10.1083/jcb.201405051. PMC 4178959. PMID 25246614 .
- ^ Michel Eduardo Beleza Yamagishi (2009). "A simpler explanation to BAK1 gene variation in Aortic and Blood tissues". arXiv:0909.2321 [q-bio.GN]。
- ^ “BAK1 gene variation and abdominal aortic aneurysms”. Human Mutation 30 (7): 1043–7. (July 2009). doi:10.1002/humu.21046. PMID 19514060.
- ^ “BAK1 gene variation and abdominal aortic aneurysms-variants are likely due to sequencing of a processed gene on chromosome 20”. Human Mutation 31 (1): 108–9; author reply 110–1. (January 2010). doi:10.1002/humu.21147. PMID 19847788.
- ^ “Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3”. Cell 116 (4): 527–40. (February 2004). doi:10.1016/s0092-8674(04)00162-x. PMID 14980220.
- ^ “Discovery of small-molecule inhibitors of Bcl-2 through structure-based computer screening”. Journal of Medicinal Chemistry 44 (25): 4313–24. (December 2001). doi:10.1021/jm010016f. PMID 11728179.
- ^ “Towards a proteome-scale map of the human protein-protein interaction network”. Nature 437 (7062): 1173–8. (October 2005). Bibcode: 2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
- ^ “Development of a high-throughput fluorescence polarization assay for Bcl-x(L)”. Analytical Biochemistry 307 (1): 70–5. (August 2002). doi:10.1016/s0003-2697(02)00028-3. PMID 12137781.
- ^ “High-throughput methods to detect dimerization of Bcl-2 family proteins”. Analytical Biochemistry 322 (2): 170–8. (November 2003). doi:10.1016/j.ab.2003.07.014. PMID 14596824.
- ^ a b “Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins”. Genes & Development 19 (11): 1294–305. (June 2005). doi:10.1101/gad.1304105. PMC 1142553. PMID 15901672 .
- ^ “Death by design: the big debut of small molecules”. Nature Cell Biology 3 (2): E43–6. (February 2001). doi:10.1038/35055145. PMID 11175758.
- ^ a b “Fatal liaisons of p53 with Bax and Bak”. Nature Cell Biology 6 (5): 386–8. (May 2004). doi:10.1038/ncb0504-386. PMID 15122264.
- ^ “Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells”. The Journal of Biological Chemistry 280 (11): 10491–500. (March 2005). doi:10.1074/jbc.M412819200. PMID 15637055.
- ^ “MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain”. The Journal of Biological Chemistry 275 (33): 25255–61. (August 2000). doi:10.1074/jbc.M909826199. PMID 10837489.
関連 文献
[- “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. (2007). doi:10.4161/auto.2730. PMID 16874066.
- “Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K”. Nature 374 (6524): 731–3. (April 1995). Bibcode: 1995Natur.374..731F. doi:10.1038/374731a0. PMID 7715729.
- “A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions”. The EMBO Journal 14 (22): 5589–96. (November 1995). doi:10.1002/j.1460-2075.1995.tb00246.x. PMC 394673. PMID 8521816 .
- “Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis”. Science 275 (5302): 983–6. (February 1997). doi:10.1126/science.275.5302.983. PMID 9020082.
- “A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members”. The Journal of Biological Chemistry 272 (17): 11350–5. (April 1997). doi:10.1074/jbc.272.17.11350. PMID 9111042.
- “The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4”. The EMBO Journal 17 (4): 1029–39. (February 1998). doi:10.1093/emboj/17.4.1029. PMC 1170452. PMID 9463381 .
- “Genomic structure and domain organisation of the human Bak gene”. Gene 211 (1): 87–94. (April 1998). doi:10.1016/S0378-1119(98)00101-2. PMID 9573342.
- “Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria”. Proceedings of the National Academy of Sciences of the United States of America 95 (25): 14681–6. (December 1998). Bibcode: 1998PNAS...9514681N. doi:10.1073/pnas.95.25.14681. PMC 24509. PMID 9843949 .
- “Boo, a novel negative regulator of cell death, interacts with Apaf-1”. The EMBO Journal 18 (1): 167–78. (January 1999). doi:10.1093/emboj/18.1.167. PMC 1171112. PMID 9878060 .
- “Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis”. The Journal of Cell Biology 144 (5): 903–14. (March 1999). doi:10.1083/jcb.144.5.903. PMC 2148192. PMID 10085290 .
- “Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC”. Nature 399 (6735): 483–7. (June 1999). Bibcode: 1999Natur.399..483S. doi:10.1038/20959. PMID 10365962.
- “A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region”. Cell Death and Differentiation 6 (4): 314–25. (April 1999). doi:10.1038/sj.cdd.4400493. PMID 10381623.
- “Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members”. Cell Death and Differentiation 6 (6): 525–32. (June 1999). doi:10.1038/sj.cdd.4400519. PMID 10381646.
- “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. (December 1999). doi:10.1210/en.140.12.5469. PMID 10579309.
- “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”. Proceedings of the National Academy of Sciences of the United States of America 97 (2): 577–82. (January 2000). Bibcode: 2000PNAS...97..577S. doi:10.1073/pnas.97.2.577. PMC 15372. PMID 10639121 .
- “MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain”. The Journal of Biological Chemistry 275 (33): 25255–61. (August 2000). doi:10.1074/jbc.M909826199. PMID 10837489.
- “tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c”. Genes & Development 14 (16): 2060–71. (August 2000). PMC 316859. PMID 10950869 .
- “Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL”. Nature Cell Biology 3 (2): 173–82. (February 2001). doi:10.1038/35055085. PMID 11175750.
- “Suppression of apoptosis, crypt hyperplasia, and altered differentiation in the colonic epithelia of bak-null mice”. Gastroenterology 136 (3): 943–52. (March 2009). doi:10.1053/j.gastro.2008.11.036. PMID 19185578 .
外部 リンク
[- Human BAK1 genome location and BAK1 gene details page in the UCSC Genome Browser.