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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

BCL2/adenovirus E1B 19kDa interacting protein 3

BNIP3, Nip3
This gene is a member of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. It interacts with the E1B 19 kDa protein, which protects cells from virally-induced cell death. The encoded protein also interacts with E1B 19 kDa-like sequences of BCL2, another apoptotic protector. This protein 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. [provided by RefSeq, Mar 2011] (from NCBI)
Top mentioned proteins: bcl-2, PrP, CAN, HIF-1alpha, V1a
Papers using BNIP3 antibodies
Association of RB/p16-pathway perturbations with DCIS recurrence: dependence on tumor versus tissue microenvironment
Lisanti Michael P. et al., In Cell Cycle, 2010
... follows: β-actin (Sigma-Aldrich, #A5441); Cav-1 mAb 2297 (BD Transduction Laboratories, #610406); Beclin1 (Novus Biologicals, #NBP1-00085); BNIP3 (Abcam, #ab10433); BNIP3L (Abcam, #ab8399); ...
Aging: past, present and future
Lisanti Michael P. et al., In Cell Cycle, 2008
... were as follows: β-actin (Sigma-Aldrich, #A5441); Cav-1 (BD Transduction Laboratories, #610406); Beclin1 (Novus Biologicals, #NBP1–00085); BNIP3 (Abcam, #ab10433); Cathepsin B (FL-339) (Santa ...
Papers on BNIP3
BNIP3 is essential for mitochondrial bioenergetics during adipocyte remodelling in mice.
Park et al., Seoul, South Korea. In Diabetologia, Jan 2016
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 (BNIP3) is a mitochondrial protein and a known mitochondrial quality regulator.
BNIP3 promotes calcium and calpain-dependent cell death.
Webster et al., Miami, United States. In Life Sci, Jan 2016
Hypoxia-acidosis was demonstrated to activate the pro-apoptotic Bcl-2 protein BNIP3 which initiated opening of the mitochondrial permeability transition pore and cell death in the absence of caspase activation.
Mieap-regulated mitochondrial quality control is frequently inactivated in human colorectal cancer.
Arakawa et al., Tokyo, Japan. In Oncogenesis, Dec 2015
BNIP3 and NIX are critical mediators for the Mieap-regulated mitochondrial quality control.
Human Milk Fortification Increases Bnip3 Expression Associated With Intestinal Cell Death In Vitro.
Friel et al., Winnipeg, Canada. In J Pediatr Gastroenterol Nutr, Nov 2015
HMF increases the expression of BCL2/adenovirus E1B 19 kDa protein-interacting protein (Bnip3) and cell death; the prostaglandin analogue misoprostol will rescue this effect.
Bcl-2 family member Mcl-1 expression is reduced under hypoxia by the E3 ligase FBW7 contributing to BNIP3 induced cell death in glioma cells.
Gibson et al., Winnipeg, Canada. In Cancer Biol Ther, Nov 2015
Hypoxic regions of GBM also highly express the pro-cell death Bcl-2 family member BNIP3, yet when BNIP3 is over-expressed in glioma cells, it induces cell death.
Tumor suppressor functions of BNIP3 and mitophagy.
Macleod et al., Chicago, United States. In Autophagy, Nov 2015
Our recent work adds to this appreciation by showing that the mitophagy receptor BNIP3 functions as a tumor suppressor in mammary tumorigenesis and also as a prognostic indicator of progression to metastasis in certain sub-types of human breast cancer.
Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses.
Chen et al., Beijing, China. In Biochim Biophys Acta, Oct 2015
In mammals, different mitophagy effectors, including the mitophagy receptors NIX, BNIP3 and FUDNC1 and the PINK1/Parkin pathway, have been identified to participate in the selective clearance of mitochondria.
Mitochondrial autophagy: Origins, significance, and role of BNIP3 and NIX.
Ney, New York City, United States. In Biochim Biophys Acta, Oct 2015
BNIP3 and NIX are related multi-functional outer mitochondrial membrane proteins.
Effects of long-term resistance exercise training on autophagy in rat skeletal muscle of chloroquine-induced sporadic inclusion body myositis.
Yeom et al., Pensacola, United States. In J Exerc Nutrition Biochem, Sep 2015
Although CQ-treatment groups suppressed the levels of the potent autophagy inducer, BNIP3, p62 levels were decreased in only the CE group.
BNIP3- and BNIP3L-Mediated Mitophagy Promotes the Generation of Natural Killer Cell Memory.
Sun et al., New York City, United States. In Immunity, Sep 2015
Furthermore, we demonstrated a temporally regulated role for mitophagy-inducing proteins BCL2/adenovirus E1B 19-kDa interacting protein 3 (BNIP3) and BNIP3-like (BNIP3L) in the generation of robust NK cell memory.
The divergent roles of autophagy in ischemia and preconditioning.
Qin et al., Suzhou, China. In Acta Pharmacol Sin, Apr 2015
Preconditioning or lethal ischemia may trigger autophagy via multiple signaling pathways involving endoplasmic reticulum (ER) stress, AMPK/TSC/mTOR, Beclin 1/BNIP3/SPK2, and FoxO/NF-κB transcription factors, etc. Autophagy then interacts with apoptotic and necrotic signaling pathways to regulate cell death.
The role of STAT3 in autophagy.
Han et al., Hangzhou, China. In Autophagy, 2014
For example, nuclear STAT3 fine-tunes autophagy via the transcriptional regulation of several autophagy-related genes such as BCL2 family members, BECN1, PIK3C3, CTSB, CTSL, PIK3R1, HIF1A, BNIP3, and microRNAs with targets of autophagy modulators.
Macrophage migration inhibitory factor has a permissive role in concanavalin A-induced cell death of human hepatoma cells through autophagy.
Yeh et al., Tainan City, Taiwan. In Cell Death Dis, 2014
Furthermore, signal pathway studies demonstrated that ConA induces signal transducer and activator of transcription 3 (STAT3) phosphorylation to trigger MIF upregulation, which in turn promotes Bcl-2/adenovirus E1B 19 kDa-interacting protein 3 (BNIP3)-dependent autophagy.
Bnip3 and AIF cooperate to induce apoptosis and cavitation during epithelial morphogenesis.
Li et al., New Brunswick, United States. In J Cell Biol, 2012
These results uncover a mechanism of cavitation through hypoxia-induced apoptosis of the core cells mediated by HIFs, Bnip3, and AIF.
BNip3 regulates mitochondrial function and lipid metabolism in the liver.
Macleod et al., Chicago, United States. In Mol Cell Biol, 2012
Loss of BNip3 resulted in increased lipid synthesis in the liver that was associated with elevated ATP levels, reduced AMP-regulated kinase (AMPK) activity, and increased expression of lipogenic enzymes.
Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy.
Gustafsson et al., San Diego, United States. In J Biol Chem, 2012
Bnip3 induced removal of both ER (ERphagy) and mitochondria (mitophagy) via autophagy. The clearance of these organelles was mediated in part via binding of Bnip3 to LC3 on the autophagosome.
Differential expression of BNIP family members of BH3-only proteins during the development and after axotomy in the rat.
Geum et al., Seoul, South Korea. In Mol Cells, 2012
three members of the BNIP family, BNIP1, BNIP3 and BNIP3L, are expressed in the developing brain with distinct brain region specificity
Expression TGM2 and BNIP3 have prognostic significance in laryngeal cancer patients receiving surgery and postoperative radiotherapy: a retrospective study.
Hu et al., Hangzhou, China. In J Transl Med, 2011
BNIP3 expression and TGM2 expression are independent prognostic factors in laryngeal SCC patients receiving postoperative radiotherapy.
Mechanisms of mitophagy.
Narendra et al., Bethesda, United States. In Nat Rev Mol Cell Biol, 2011
Mitophagy, the specific autophagic elimination of mitochondria, has been identified in yeast, mediated by autophagy-related 32 (Atg32), and in mammals during red blood cell differentiation, mediated by NIP3-like protein X (NIX; also known as BNIP3L).
Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins.
Chinnadurai et al., Saint Louis, United States. In Cell, 1994
We have isolated cDNAs for three different proteins, designated Nip1, Nip2, and Nip3, that interact with the 19 kDa protein.
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