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BCL2/ADENOVIRUS E1B 19-KD PROTEIN-INTERACTING PROTEIN 3-LIKE; BNIP3L

BCL2/ADENOVIRUS E1B 19-KD PROTEIN-INTERACTING PROTEIN 3-LIKE; BNIP3L

Alternative titles; symbolsNIXHGNC Approved Gene Symbol: BNIP3LCytogenetic location: 8p21.2 Genomic coordinates (GRCh38): 8:26,383,053-26,413,126 (from NCBI)...

Alternative titles; symbols

  • NIX

HGNC Approved Gene Symbol: BNIP3L

Cytogenetic location: 8p21.2 Genomic coordinates (GRCh38): 8:26,383,053-26,413,126 (from NCBI)

▼ Cloning and Expression
In a large-scale sequencing effort of randomly selected cDNA clones, Matsushima et al. (1998) identified BNIP3L as a homolog of the previously identified proapoptotic protein BNIP3 (603293). Chen et al. (1999) and Yasuda et al. (1999) also identified BNIP3L sequences in database searches for sequences homologous to BNIP3. BNIP3L encodes a deduced 219-amino acid protein that contains a predicted transmembrane domain, PEST sequences, and a BH3 domain in the C-terminal region. BNIP3L shares 56% amino acid sequence identity with BNIP3. Chen et al. (1999) predicted that BNIP3L forms a homodimer because the observed 48-kD protein product is about double the 23.8-kD predicted mass. By Northern blot analysis, Matsushima et al. (1998) detected a 1.45-kb BNIP3L transcript in all tissues examined, and Yasuda et al. (1999) detected 1.6- and 3.9-kb transcripts in all tissues examined but at lower levels in liver, skeletal muscle, and pancreas.

▼ Gene Function
Using indirect immunofluorescence analysis of an epitope-tagged BNIP3L, Yasuda et al. (1999) localized BNIP3L to mitochondria. Chen et al. (1999) colocalized BNIP3L with the 60-kD heat-shock protein-1 (HSPD1; 118190) known to be located primarily in mitochondria. The localization of BNIP3L to the mitochondria is dependent on the putative transmembrane domain.

Consistent with the presence of PEST sequences, which are associated with proteins having high turnover rates whose degradation is controlled by the proteasome, Chen et al. (1999) found that BNIP3L is progressively degraded over 42 hours following transfection. This proteolytic degradation is dependent on an active proteasome and is inhibited with lactacystin, the proteasome threonine protease inhibitor.

Matsushima et al. (1998) used colony formation assays to demonstrate that transient overexpression of BNIP3L caused a suppression of cancer cell growth. Chen et al. (1999) noted that this growth suppression can be accounted for by the proapoptotic function proposed for BNIP3L. Yasuda et al. (1999) and Chen et al. (1999) observed that BNIP3L transfection induces apoptosis. Chen et al. (1999) demonstrated that removal of the transmembrane domain prevents the cell death induction. Additionally, BNIP3L expression can overcome the effect of the antiapoptotic BCL2 (151430) and BCL2L1 (600039) in transfected cells.

Yasuda et al. (1999) showed that in vitro translated BNIP3L binds specifically and directly with GST fusion proteins of various BCL2 family antiapoptosis proteins including BCL2, BCL2L1, and adenovirus E1B 19-kD. Cotransfection of BNIP3L significantly reduced the antiapoptotic activity of E1B 19-kD and BCL2L1, leading Yasuda et al. (1999) to suggest that, like BNIP3, BNIP3L may antagonize the activity of BCL2 family antiapoptosis proteins.

PARK2 (602544) is an E3 ubiquitin ligase that ubiquitinates proteins on damaged mitochondria, targeting the mitochondria for lysosomal degradation. Gao et al. (2015) identified BNIP3L as a mitochondrial PARK2 substrate and showed that ubiquitinated BNIP3L recruited cytosolic NBR1 (166945) to damaged mitochondria, thereby targeting the organelle for degradation. Knockdown of either NBR1 or BNIP3L in HEK293A cells disrupted degradation of mitochondria damaged by inhibition of oxidative phosphorylation. In contrast, inhibition of mitochondrial complex I induced BNIP3L degradation and caused retention of damaged mitochondria.

▼ Mapping
By FISH, Matsushima et al. (1998) mapped the BNIP3L gene to 8p21. The authors noted that this region shows frequent loss of heterozygosity in carcinomas of the colon, prostate, liver, and lung.

▼ Animal Model
Sandoval et al. (2008) generated mice deficient in Nix1 by targeted disruption. Nix-null mice developed anemia with reduced mature erythrocytes and compensatory expansion of erythroid precursors. Erythrocytes in the peripheral blood of Nix-null mice exhibited mitochondrial retention and reduced life span in vivo. Although the clearance of ribosomes proceeded normally in the absence of Nix, the entry of mitochondria into autophagosomes for clearance was defective. Deficiency in Nix inhibited the loss of mitochondrial membrane potential, and treatment with uncoupling chemicals or a BH3 mimetic induced the loss of mitochondrial membrane potential and restored the sequestration of mitochondria into autophagosomes in Nix-null erythroid cells. Sandoval et al. (2008) concluded that Nix-dependent loss of mitochondrial membrane potential is important for targeting the mitochondria into autophagosomes for clearance during erythroid maturation, and interference with this function impairs erythroid maturation and results in anemia.

Tags: 8p21.2

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