Table 2 The involvement of BNIP3L in human disease.

Cancer

Melanoma

BNIP3L causes autophagic melanoma cell death by recruiting TR3 to mitochondria

[55]

Glioma

BNIP3L participates in the mitophagic glioma cell death caused by AT 101

[114]

Ewing sarcoma

Degradation of endogenous BNIP3L is required for the survival of Ewing sarcoma cells

[68]

Acute myeloid leukemia

BNIP3L expression as a useful prognostic marker of acute myeloid leukemia

[115]

Solid tumor (cell lines)

Autophagy via BNIP3L promotes tumors

[42, 43]

Breast cancer

Upregulation of BNIP3L linked with TNF-α resistance

[32, 116]

Upregulation of BNIP3L delays mitophagic apoptosis

Glioblastoma

BNIP3L-induced mitophagy reduces oxidative damage and promotes glioblastoma cell survival

[117]

Pancreatic cancer

Deletion of Bnip3l delays the progression of pancreatic cancer

[118]

Neurodegeneration

Parkinson’s disease

BNIP3L compensates for mitophagic defects in PD patient-derived cells

[59, 122]

Amyotrophic lateral sclerosis

Upregulation of BNIP3L may promote ALS progression via a non-apoptotic function

[127]

Acute brain injury

Cerebral ischemia

BNIP3L protects against cerebral ischemia via mitophagy. The inhibition of BNIP3L degradation by carfilzomib attenuates cerebral ischemia.

[15, 16]

Traumatic brain injury

Bnip3l overexpression enhances autophagic flux and attenuates traumatic brain injury

[60]

Intracerebral hemorrhage

BNIP3L is upregulated in intracerebral hemorrhage rats. The increased interaction between BNIP3L and p75 promotes neuronal apoptosis

[137, 138]