Просмотр кода страницы Английская Википедия:BH3 interacting-domain death agonist

{{Английская Википедия/Панель перехода}}
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
{{Infobox protein family
| Symbol = BID
| Name = BID
| image = PDB 2bid EBI.jpg
| width = 
| caption = human pro-apoptotic protein bid
| Pfam = PF06393
| Pfam_clan =  
| InterPro = IPR010479
| SMART = 
| PROSITE = 
| MEROPS = 
| SCOP = 1ddb
| TCDB = 1.A.21
| OPM family = 40
| OPM protein = 2m5i
| CAZy = 
| CDD = 
}}
The '''BH3 interacting-domain death agonist''', or '''BID''', [[gene]] is a pro-[[apoptosis|apoptotic]] member of the [[Bcl-2]] protein family.<ref name="pmid8918887">{{cite journal | vauthors = Wang K, Yin XM, Chao DT, Milliman CL, Korsmeyer SJ | title = BID: a novel BH3 domain-only death agonist | journal = Genes Dev. | volume = 10 | issue = 22 | pages = 2859–69 | year = 1996 | pmid = 8918887 | doi = 10.1101/gad.10.22.2859 | doi-access = free }}</ref> Bcl-2 family members share one or more of the four characteristic [[Domain (biology)|domain]]s of [[Homology (biology)|homology]] entitled the Bcl-2 homology (BH) domains (named BH1, BH2, [[BH3 domain|BH3]] and BH4), and can form hetero- or homodimers. Bcl-2 proteins act as anti- or pro-[[apoptosis|apoptotic]] regulators that are involved in a wide variety of cellular activities.

==Interactions==
BID is a pro-apoptotic Bcl-2 protein containing only the BH3 domain. In response to apoptotic signaling, BID interacts with another Bcl-2 family [[protein]], [[Bcl-2-associated X protein|Bax]], leading to the insertion of Bax into [[organelle]] membranes, primarily the outer [[mitochondria]]l membrane.  Bax is believed to interact with, and induce the opening of the mitochondrial voltage-dependent anion channel, [[voltage-dependent anion channel|VDAC]]. Alternatively, growing evidence suggest that activated Bax and/or [[Bcl-2 homologous antagonist killer|Bak]] form an oligomeric pore, [[MAC, the Mitochondrial Apoptosis-Induced Channel|MAC]] in the outer membrane.  This results in the release of cytochrome c and other pro-apoptotic factors (such as [[Diablo homolog|SMAC]]/DIABLO)<ref>{{cite book|last=Weinberg|first=Robert A.|title=The biology of cancer|year=2007|publisher=Taylor & Francis|location=New York|isbn=978-0-8153-4076-8|pages=341}}</ref> from the mitochondria, often referred to as mitochondrial outer membrane permeabilization, leading to activation of [[caspases]]. This defines BID as a direct activator of Bax, a role common to some of the pro-apoptotic  Bcl-2 proteins containing only the BH3 domain.

The anti-apoptotic Bcl-2 proteins, including Bcl-2 itself, can bind BID and inhibit BID's ability to activate Bax. As a result, the anti-apoptotic Bcl-2 proteins may inhibit apoptosis by sequestering BID, leading to reduced Bax activation.

The expression of ''BID'' is upregulated by the [[tumor suppressor gene|tumor suppressor]] [[p53]], and BID has been shown to be involved in p53-mediated apoptosis.<ref name="pmid12402042">{{cite journal | vauthors = Sax JK, Fei P, Murphy ME, Bernhard E, Korsmeyer SJ, El-Deiry WS | title = BID regulation by p53 contributes to chemosensitivity | journal = Nat. Cell Biol. | volume = 4 | issue = 11 | pages = 842–9 | year = 2002 | pmid = 12402042 | doi = 10.1038/ncb866 | s2cid = 2206946 }}</ref> The p53 protein is a [[transcription factor]] that, when activated as part of the cell's response to stress, regulates many downstream target genes, including ''BID''. However, p53 also has a transcription-independent role in apoptosis. In particular, p53 interacts with [[Bcl-2-associated X protein|Bax]], promoting Bax activation and the insertion of Bax into the mitochondrial membrane.

The BH3 interacting-domain death agonist has been shown to [[Protein-protein interaction|interact]] with:
* [[Ataxia telangiectasia and Rad3 related|ATR]]/ATRIP,<ref name = pmid21113148>{{cite journal | vauthors = Liu Y, Bertram CC, Shi Q, Zinkel SS | title = Proapoptotic Bid mediates the Atr-directed DNA damage response to replicative stress | journal = Cell Death Differ. | volume = 18 | issue = 5 | pages = 841–52 | year = 2011 | pmid = 21113148 | pmc = 3074003 | doi = 10.1038/cdd.2010.151 }}</ref> 
* [[Bcl-2|BCL2]],<ref name = pmid15694340>{{cite journal | vauthors = Chen L, Willis SN, Wei A, Smith BJ, Fletcher JI, Hinds MG, Colman PM, Day CL, Adams JM, Huang DC | title = Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function | journal = Mol. Cell | volume = 17 | issue = 3 | pages = 393–403 | year = 2005 | pmid = 15694340 | doi = 10.1016/j.molcel.2004.12.030 | doi-access = free }}</ref><ref name = pmid15520201>{{cite journal | vauthors = Real PJ, Cao Y, Wang R, Nikolovska-Coleska Z, Sanz-Ortiz J, Wang S, Fernandez-Luna JL | title = Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2 | journal = Cancer Res. | volume = 64 | issue = 21 | pages = 7947–53 | year = 2004 | pmid = 15520201 | doi = 10.1158/0008-5472.CAN-04-0945 | doi-access = free }}</ref> 
* [[Caspase 2|CASP2]],<ref name = pmid11832478/><ref name = pmid11399776>{{cite journal | vauthors = Paroni G, Henderson C, Schneider C, Brancolini C | title = Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3 | journal = J. Biol. Chem. | volume = 276 | issue = 24 | pages = 21907–15 | year = 2001 | pmid = 11399776 | doi = 10.1074/jbc.M011565200 | doi-access = free }}</ref> 
* [[Caspase 8|CASP8]],<ref name = pmid11832478>{{cite journal | vauthors = Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES | title = Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria | journal = J. Biol. Chem. | volume = 277 | issue = 16 | pages = 13430–7 | year = 2002 | pmid = 11832478 | doi = 10.1074/jbc.M108029200 | doi-access = free }}</ref><ref name = pmid15659383>{{cite journal | vauthors = Gajate C, Mollinedo F | title = Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy | journal = J. Biol. Chem. | volume = 280 | issue = 12 | pages = 11641–7 | year = 2005 | pmid = 15659383 | doi = 10.1074/jbc.M411781200 | doi-access = free }}</ref>
* [[MCL1]],<ref name = pmid15694340/><ref name = pmid15637055>{{cite journal | vauthors = Weng C, Li Y, Xu D, Shi Y, Tang H | title = Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells | journal = J. Biol. Chem. | volume = 280 | issue = 11 | pages = 10491–500 | year = 2005 | pmid = 15637055 | doi = 10.1074/jbc.M412819200 | doi-access = free }}</ref>  and
* [[Replication protein A|RPA]].<ref name = pmid21859891>{{cite journal | vauthors = Liu Y, Vaithiyalingam S, Shi Q, Chazin WJ, Zinkel SS | title = BID binds to replication protein A and stimulates ATR function following replicative stress | journal = Mol. Cell. Biol. | volume = 31 | issue = 21 | pages = 4298–309 | year = 2011 | pmid = 21859891 | pmc = 3209332 | doi = 10.1128/MCB.05737-11 }}</ref>

==Cleavage==
[[File:Casp8-BID.gif|thumb|300px|Caspase-8 (as surface) cleavage of Bid (as ribbon) (visualization by [https://web.archive.org/web/20070125074628/http://pmap.burnham.org/www/pmap4/html/index.html Kosi Gramatikoff])]]

Several reports have demonstrated that [[caspase]]-8, and its substrate BID, are frequently activated in response to certain [[apoptotic]] stimuli in a death receptor-independent manner. N-hydroxy-L-arginine (NOHA), a stable intermediate product formed during the conversion of L-arginine to [[nitric oxide]] activates caspase-8.<ref name="pmid12145284">{{cite journal | vauthors = Singh R, Pervin S, Chaudhuri G | title = Caspase-8-mediated BID cleavage and release of mitochondrial cytochrome c during Nomega-hydroxy-L-arginine-induced apoptosis in MDA-MB-468 cells. Antagonistic effects of L-ornithine | journal = J. Biol. Chem. | volume = 277 | issue = 40 | pages = 37630–6 | year = 2002 | pmid = 12145284 | doi = 10.1074/jbc.M203648200 | doi-access = free }}</ref> Activation of caspase-8, and subsequent BID cleavage  participate in [[cytochrome-c]] mediated [[apoptosis]].<ref name="pmid10734071">{{cite journal | vauthors = Tang D, Lahti JM, Kidd VJ | title = Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis | journal = J. Biol. Chem. | volume = 275 | issue = 13 | pages = 9303–7 | year = 2000 | pmid = 10734071 | doi = 10.1074/jbc.275.13.9303 | doi-access = free }}</ref> 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mediated activation of caspase-9 via [[cytochrome-c]] release has been shown to result in the activation of caspase-8 and Bid cleavage.<ref name="pmid11739563">{{cite journal | vauthors = Viswanath V, Wu Y, Boonplueang R, Chen S, Stevenson FF, Yantiri F, Yang L, Beal MF, Andersen JK | title = Caspase-9 activation results in downstream caspase-8 activation and bid cleavage in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson's disease | journal = J. Neurosci. | volume = 21 | issue = 24 | pages = 9519–28 | year = 2001 | pmid = 11739563 | doi = 10.1523/JNEUROSCI.21-24-09519.2001| pmc = 6763046 | doi-access = free }}</ref> [[Aspirin]] and [[Curcumin]] (diferuloylmethane) too activate caspase-8 to cleave and translocate Bid, induced a conformational change in and translocation of Bax and [[cytochrome-c]] release.<ref name="pmid15579484">{{cite journal | vauthors = Gu Q, Wang JD, Xia HH, Lin MC, He H, Zou B, Tu SP, Yang Y, Liu XG, Lam SK, Wong WM, Chan AO, Yuen MF, Kung HF, Wong BC | title = Activation of the caspase-8/Bid and Bax pathways in aspirin-induced apoptosis in gastric cancer | journal = Carcinogenesis | volume = 26 | issue = 3 | pages = 541–6 | year = 2005 | pmid = 15579484 | doi = 10.1093/carcin/bgh345 | doi-access = free }}</ref><ref name="pmid11756235">{{cite journal | vauthors = Anto RJ, Mukhopadhyay A, Denning K, Aggarwal BB | title = Curcumin (diferuloylmethane) induces apoptosis through activation of caspase-8, BID cleavage and cytochrome c release: its suppression by ectopic expression of Bcl-2 and Bcl-xl | journal = Carcinogenesis | volume = 23 | issue = 1 | pages = 143–50 | year = 2002 | pmid = 11756235 | doi = 10.1093/carcin/23.1.143 | doi-access = free }}</ref>

==See also==
{{columns-list|colwidth=30em|
* [[Apoptosis]]
* [[Apoptosome]]
* [[Bcl-2]]
* [[Bcl-2-associated X protein]] (BAX)
* [[Caspases]]
* [[Cytochrome c]]
* [[Noxa]]
* [[Mitochondrion]]
* [[p53 upregulated modulator of apoptosis]] (PUMA)
}}

==References==
{{Reflist}}

==External links==
* {{UCSC gene info|BID}}

{{Fas apoptosis signaling pathway}}

{{DEFAULTSORT:Bh3 Interacting-Domain Death Agonist}}
[[Category:Apoptosis]]
[[Category:Programmed cell death]]
[[Category:Proteins]]
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