1. Structure

2. Function
     Transport reaction  

3. Interactions

4. References

5. Further reading

6. External links

BNIP3 is a member of the apoptotic Bcl-2 protein family that is involved an atypical programmed cell death pathway resembling both necrosis and apoptosis. Many Bcl-2 family proteins modulate the permeability state of the outer mitochondrial membrane by forming homo- and hetero-oligomers. However, sequence similarity with Bcl-2 family members was not detected. Humans and other animals (Drosophila, Caenorhabditis), as well as lower eukaryotes (Dictyostelium, Trypanosoma, Cryptosporidium, Paramecium) encode several BNIP3 paralogues including the human NIP3L, which induces apoptosis by interacting with viral and cellular anti-apoptosis proteins.

Structure

The right-handed parallel helix-helix structure of the domain with a hydrogen bond-rich His-Ser node in the middle of the membrane, accessibility of the node for water, and continuous hydrophilic track across the membrane suggest that the domain can provide an ion-conducting pathway through the membrane. Incorporation of the BNIP3 transmembrane domain into an artificial lipid bilayer resulted in a pH-dependent conductivity increase. Necrosis-like cell death induced by BNIP3 may be related to this activity.^[2]

Function

BNIP3 interacts with the E1B 19 kDa protein which is responsible for the protection of virally induced cell death, as well as E1B 19 kDa-like sequences of BCL2, also an apoptotic protector. This gene contains a BH3 domain and a transmembrane domain, which have been associated with pro-apoptotic function. The dimeric mitochondrial protein encoded by this gene is known to induce apoptosis, even in the presence of BCL2.^[3] Change of BNIP3 expression along other members of the Bcl-2 family measured by qPCR captures important characteristics of malignant transformation, and are defined as markers of resistance toward cell death, a key Cancer Hallmark.^[4]

Transport reaction

The reaction catalyzed by BNIP3 is:

small molecules (out) ⇌ small molecules (in)

Interactions

BNIP3 has been shown to interact with CD47,^[5] BCL2-like 1^[6] and Bcl-2.^[1][6]

References

Further reading

• {{cite journal | vauthors = Kataoka N, Ohno M, Moda I, Shimura Y | title = Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein | journal = Nucleic Acids Research | volume = 23 | issue = 18 | pages = 3638–41 | date = Sep 1995 | pmid = 7478990 | pmc = 307259 | doi = 10.1093/nar/23.18.3638 }}
• {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
• {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
• {{cite journal | vauthors = Chen G, Ray R, Dubik D, Shi L, Cizeau J, Bleackley RC, Saxena S, Gietz RD, Greenberg AH | title = The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis | journal = The Journal of Experimental Medicine | volume = 186 | issue = 12 | pages = 1975–83 | date = Dec 1997 | pmid = 9396766 | pmc = 2199165 | doi = 10.1084/jem.186.12.1975 }}
• {{cite journal | vauthors = Yasuda M, Theodorakis P, Subramanian T, Chinnadurai G | title = Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence | journal = The Journal of Biological Chemistry | volume = 273 | issue = 20 | pages = 12415–21 | date = May 1998 | pmid = 9575197 | doi = 10.1074/jbc.273.20.12415 }}
• {{cite journal | vauthors = Chen G, Cizeau J, Vande Velde C, Park JH, Bozek G, Bolton J, Shi L, Dubik D, Greenberg A | title = Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins | journal = The Journal of Biological Chemistry | volume = 274 | issue = 1 | pages = 7–10 | date = Jan 1999 | pmid = 9867803 | doi = 10.1074/jbc.274.1.7 }}
• {{cite journal | vauthors = Yasuda M, Han JW, Dionne CA, Boyd JM, Chinnadurai G | title = BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3 | journal = Cancer Research | volume = 59 | issue = 3 | pages = 533–7 | date = Feb 1999 | pmid = 9973195 | doi = }}
• {{cite journal | vauthors = Ohi N, Tokunaga A, Tsunoda H, Nakano K, Haraguchi K, Oda K, Motoyama N, Nakajima T | 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 and Differentiation | volume = 6 | issue = 4 | pages = 314–25 | date = Apr 1999 | pmid = 10381623 | doi = 10.1038/sj.cdd.4400493 }}
• {{cite journal | vauthors = Ray R, Chen G, Vande Velde C, Cizeau J, Park JH, Reed JC, Gietz RD, Greenberg AH | title = BNIP3 heterodimerizes with Bcl-2/Bcl-X(L) and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites | journal = The Journal of Biological Chemistry | volume = 275 | issue = 2 | pages = 1439–48 | date = Jan 2000 | pmid = 10625696 | doi = 10.1074/jbc.275.2.1439 }}
• {{cite journal | vauthors = Vande Velde C, Cizeau J, Dubik D, Alimonti J, Brown T, Israels S, Hakem R, Greenberg AH | title = BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore | journal = Molecular and Cellular Biology | volume = 20 | issue = 15 | pages = 5454–68 | date = Aug 2000 | pmid = 10891486 | pmc = 85997 | doi = 10.1128/MCB.20.15.5454-5468.2000 }}
• {{cite journal | vauthors = Lee SM, Li ML, Tse YC, Leung SC, Lee MM, Tsui SK, Fung KP, Lee CY, Waye MM | title = Paeoniae Radix, a Chinese herbal extract, inhibit hepatoma cells growth by inducing apoptosis in a p53 independent pathway | journal = Life Sciences | volume = 71 | issue = 19 | pages = 2267–77 | date = Sep 2002 | pmid = 12215374 | doi = 10.1016/S0024-3205(02)01962-8 }}
• {{cite journal | vauthors = Lamy L, Ticchioni M, Rouquette-Jazdanian AK, Samson M, Deckert M, Greenberg AH, Bernard A | title = CD47 and the 19 kDa interacting protein-3 (BNIP3) in T cell apoptosis | journal = The Journal of Biological Chemistry | volume = 278 | issue = 26 | pages = 23915–21 | date = Jun 2003 | pmid = 12690108 | doi = 10.1074/jbc.M301869200 }}
• {{cite journal | vauthors = Kothari S, Cizeau J, McMillan-Ward E, Israels SJ, Bailes M, Ens K, Kirshenbaum LA, Gibson SB | title = BNIP3 plays a role in hypoxic cell death in human epithelial cells that is inhibited by growth factors EGF and IGF | journal = Oncogene | volume = 22 | issue = 30 | pages = 4734–44 | date = Jul 2003 | pmid = 12879018 | doi = 10.1038/sj.onc.1206666 }}
• {{cite journal | vauthors = Okami J, Simeone DM, Logsdon CD | title = Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer | journal = Cancer Research | volume = 64 | issue = 15 | pages = 5338–46 | date = Aug 2004 | pmid = 15289340 | doi = 10.1158/0008-5472.CAN-04-0089 | citeseerx = 10.1.1.326.628 }}
• {{cite journal | vauthors = Giatromanolaki A, Koukourakis MI, Sowter HM, Sivridis E, Gibson S, Gatter KC, Harris AL | title = BNIP3 expression is linked with hypoxia-regulated protein expression and with poor prognosis in non-small cell lung cancer | journal = Clinical Cancer Research | volume = 10 | issue = 16 | pages = 5566–71 | date = Aug 2004 | pmid = 15328198 | doi = 10.1158/1078-0432.CCR-04-0076 }}
• {{cite journal | vauthors = Shen XY, Zacal N, Singh G, Rainbow AJ | title = Alterations in mitochondrial and apoptosis-regulating gene expression in photodynamic therapy-resistant variants of HT29 colon carcinoma cells | journal = Photochemistry and Photobiology | volume = 81 | issue = 2 | pages = 306–13 | year = 2005 | pmid = 15560738 | doi = 10.1562/2004-07-22-RA-242 }}

External links

• {{UCSC gene info|BNIP3}}

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