This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
2 Citations 3 Q&As
Facts about BCL2/adenovirus E1B 19 kDa protein-interacting protein 3.
Involved in mitochondrial quality control through its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) resulting in the degradation of damaged proteins within mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX in the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins in the cytoplasm to the mitochondrial matrix.
Human | |
---|---|
Gene Name: | BNIP3 |
Uniprot: | Q12983 |
Entrez: | 664 |
Belongs to: |
---|
NIP3 family |
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3; BCL2/adenovirus E1B 19kDa interacting protein 3; BCL2/adenovirus E1B 19kD-interacting protein 3; BNIP3; Nip3
Mass (kDA):
27.832 kDA
Human | |
---|---|
Location: | 10q26.3 |
Sequence: | 10; NC_000010.11 (131967683..131982013, complement) |
Mitochondrion. Mitochondrion outer membrane; Single-pass membrane protein. Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane.
In this article, we'll review the BNIP3 domain's functions in mitochondrial targeting and Bcl-2 (L) heterodimerization. We will also examine the advantages of this antibody for your research. Learn more about what makes it a useful product. Boster Bio The Best Uses for the BNIP3 Marker
Transmembrane domains are (TM) found in the BNIP3 protein that is essential for homodimerization and pro-apoptotic activity. It is also involved in cell death pathways such as autophagy, necrosis-like cell death, epithelial-mesenchymal transition, and metastasis. Oncogenes control the amount of BNIP3 and influence the fate of cells through its effects on glycolysis and lipid metabolism as and mitochondrial bioenergetics. It is an essential link between life and death.
It is not clear whether BNIP3 itself induces cell death, or whether a co-expressed form of the protein is required to do this. Both Nix and BNIP3 play a similar role in the process of inducing cell death, although the mechanism may vary according to cell type and experimental conditions. BNIP3 is believed to enter the mitochondrial outer membrane and open the MPTP which results in loss in Dpsm and subsequent death. BAX and BAK are also involved in the death of cells induced by BNIP3 and their role in MPTP opening isn't fully understood.
BNIP3 has a dual function in mitophagy. It plays a role in autophagy through activating mitochondrial priming as well as reactive oxygen-mediated autophagy. Furthermore, it plays an important role in post-infarction remodeling. In addition, BNIP3 is a sequence-specific dimer, allowing it to play a pro-apoptotic role in the death of cells.
The BH3-domain of BNIP3 is essential to perform pro-apoptotic functions. Induction of cell death is triggered by activation of the Bcl-2 family, but BNIP3 isn't clear on its role in lung cancer. However it has been examined in a variety of review articles and studies on various types of cancer. Its role in lung cancer is likely to need to be studied more thoroughly and targeted therapy may be possible.
BNIP3 interacts with Rheb, which is a protein that is positively regulated upstream from mTOR. Overexpressing BNIP3 in NIX-KO reticulocytes restored mitochondrial clearance. Additionally, the LIR motif in BNIP3 is phosphorylated on two serine residues which increases its binding to LC3B and regulates mitophagy.
BNIP3 homology domain 3 (BH3-domain) is found in both pro-apoptotic as well as pro-survival Bcl-2 proteins. It can autonomously dimerize. BNIP3 has a tryptophan residue that decreases its ability to select when it is in contact with the pro-survival Bcl-2 protein. Studies have shown that BNIP3 homodimerization causes the death of cells.
The regulation of metabolic lipids as well as the process of apoptosis in cells is supported by the BNIP3 TMC domain. BNIP3 MRNA levels were significantly higher in diabetic patients, and the overexpression or deregulation of BNIP3 inhibited cardiac apoptosis. Further studies on BNIP3 is required to determine its potential target and drug candidates.
These homodimerizations are not coupled in vitro, suggesting that the BNIP3 motif is the one responsible for interactions between BCL-XL and MCL1. This conclusion was confirmed by studies of saturation mutagenesis, in which a mutation of F159 to valine increased affinity of the peptide to MCL1 and also gave preference to MCL1 over BCLXL. BCLXL interactions can also be mediated by sequences that contain phenylalanine and/or the tyrosine component in HP1.
The expression of the BNIP3 gene is observed. Different cancers express BNIP3 in different ways. The presence of BNIP3 in cancers of the lung is not related to the patient's 5-year survival. These results suggest that BNIP3 is involved in the progression of lung carcinoma. This new therapy is currently being evaluated in several clinical trials.
The mitochondrial BNIP3 location is dependent on the TMdomain at the C-terminus. A mutation in the TMdomain would cause the dissolution of heterodimerization between Bcl-2 protein that is prosurvival but not its proapoptotic function. It is also crucial for BNIP3-dependent autophagy. This protein is able to block the autophagy signal and can result in an increase in the risk of dying cells caused by apoptosis.
BNIP3 overexpression causes autophagic cell death in malignant glioma cell lines. NSCLC showed that BNIP3 expression was linked to hypoxia in tumors. Arsenic trioxide also increased expression of BNIP3 and led to autophagic cell death.
BNIP3 is a key regulator of mitochondrial function in cells and cell deaths. In addition to being an essential regulator of mitochondrial targeting, BNIP3 is also implicated in ventricular myocyte apoptosis as well as hypoxia-induced cell death. It is interesting that BNIP3 expression was increased in hypoxia-induced adult rats as well as those suffering from chronic heart failure. Subcellular fractionation studies also demonstrated that BNIP3 is integrated into mitochondria during hypoxia.
To investigate the effects DOX has on vivo the effects of DOX, mutants of BNIP3 were tested. While DOX induces heart failure in mice. However, knocking out Bnip3 completely eliminates this adverse effect by restoring mitochondrial respiration and classical markers of necrosis in this model. These results suggest that DOX cardiotoxicity is a result of Bnip3's mitochondrial target activity.
These results suggest that BNIP3 Domain mediates targeting and targeting of mitochondria. It is still unclear how BNIP3 domain regulates mitochondrial targeting. BNIP3 is involved in a variety of ways in mitochondrial function, such as enhancing mitochondrial membrane potential. The function of BMIP3 is believed to be controlled by the BNIP3 TMC domain in mitochondria.
BNIP3 is required for apoptosis, necrosis, and cell death. It triggers cell death via an in-dependent caspase pathway, resulting in apoptosis, but not the release of cytochrome-c. In the same way, a pan-caspase inhibitor, zVAD-fmk, stopped the cell death caused by BNIP3 in a dose-dependent manner. Bongkrekic acids also inhibits mitochondrial defects.
The BNIP3 domain is responsible for dimerization and heterodimerization in conjunction with other proteins. BNIP3 forms a heterodimer BAX in the OMM under normal conditions. It isn't yet clear what mechanism regulates dimerization of BNIP3 or NIX. The BNIP3 domain TM mediates mitochondrial targeting and regulates autophagy.
PINK1–Parkin pathway, however, inhibits apoptosis. This pathway also reduces mitophagy. BNIP3 is able to function in conjunction with PINK1–NPD1, which may be either complementary or antagonistic. It isn't clear how this interaction affects mitophagy. However, so far the results are promising.
There are numerous benefits when using the BNIP3 marker. It permits the analysis of RNIP3 expression in cell lysates. Additionally, the use the marker is more specific, since an increase in RNIP3 expression can detect the presence of the protein. Additionally, it is not only useful for research, but also for the process of diagnosing. It is possible to predict the development and size of cancer using the BNIP3 gene, as RNIP3 levels are related to tumor size.
BNIP3 is a protein which is found in cardiomyocytes that is localized to mitochondria. BNIP3 increased expression led to significant increases in cytoplasmic cytochrome C and cleaved Caspase 3, as well as a decrease in mitochondrial membrane potential. In addition it has been observed that BNIP3 expression is upregulated during hypoxia and can contribute to cardiomyocyte cell death.
In conclusion, BNIP3 is a potential therapeutic option for patients suffering from MI. It is an important mediator in ischemia-induced myocardial death. RNIPs can be targeted to kill-effector genes through this marker. Further, Bnip3 expression is essential for a range of medical procedures, including cardiac surgery and other treatments.
The loss of BNIP3 in patients suffering from heart failure results in an increase in the growth of primary tumors and invasiveness. In MMTV-PyMT mice, BNIP3 insufficiently causes lung metastasis. These data show that BNIP3 expression correlates with the severity of HF. There are no effective treatments available for diastolicHF. A study of this marker may help to identify the best treatment options.
In the model of a rat with pressure overload HF, BNIP3 knockdown improved diastolic function and reduced interstitial fibrosis. Knockdown of BNIP3 increased LVEF, reduced myocardial apoptosis, as well as reducing the diastolic volume at the LV's end. Furthermore, the knockdown of BNIP3 attenuated mitochondrial fragmentation, which eventually led to release of Cytochrome C.
PMID: 9396766 by Chen G., et al. The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis.
PMID: 7954800 by Boyd J.M., et al. Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins.
*More publications can be found for each product on its corresponding product page