- BH3 interacting domain death agonist
The BH3 interacting domain death agonist, or BID,
gene is a pro-apoptotic member of theBcl-2 protein family.cite journal | author = 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 | issn = ] Bcl-2 family members share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains (named BH1, BH2, BH3 and BH4), and can form hetero- or homodimers. Bcl-2 proteins act as anti- or pro-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 , Bax, leading to the insertion of Bax intoorganelle membranes, primarily the outer mitochondrial membrane. Bax is believed to interact with, and induce the opening of the mitochondrial voltage-dependent anion channel, VDAC. Alternatively, growing evidence suggest that activated Bax and/or Bak form an oligomeric pore, MAC in the outer membrane. This results in the release of cytochrome c and other pro-apoptotic factors from the mitochondria, often referred to as mitochondrial outer membrane permeabilization, leading to activation ofcaspases . This defines BID as a 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
p53 , and BID has been shown to be involved in p53-mediated apoptosis.cite journal | author = 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 | issn = ] The p53 protein is atranscription 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 Bax, promoting Bax activation and the insertion of Bax into the mitochondrial membrane.Cleavage
[
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 certainapoptotic stimuli in a death receptor-independent manner. N-hydroxy-L-arginine (NOHA), a stable intermediate product formed during the conversion of L-arginine tonitric oxide activates caspase-8.cite journal | author = 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 | issn = ] Activation of caspase-8, and subsequent BID cleavage participate incytochrome-c mediatedapoptosis .cite journal | author = 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 | issn = ] 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mediated activation of caspase-9 viacytochrome-c release has been shown to results in the activation of caspase-8 and Bid cleavage.cite journal | author = 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 = | issn = | url = http://www.jneurosci.org/cgi/content/abstract/21/24/9519 ]Aspirin andCurcumin (diferuloylmethane) too activate caspase-8 to cleave and translocated Bid, induced a conformational change in and translocation of Bax andcytochrome-c release.cite journal | author = 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 | issn = ] cite journal | author = 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 | issn = ]ee also
*
Apoptosis
*Apoptosome
*Bcl-2
*Bcl-2-associated_X_protein (BAX)
*Caspases
*Cytochrome c
*Noxa
*Mitochondrion
*p53 upregulated modulator of apoptosis (PUMA)References
PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes
Wikimedia Foundation. 2010.