Evidence map›Paper›PMID 36396625›Full record

ArticleCell death & disease2022

BNIP3 phosphorylation by JNK1/2 promotes mitophagy via enhancing its stability under hypoxia.

Yun-Ling He, Jian Li, Sheng-Hui Gong, Xiang Cheng, Ming Zhao, Yan Cao, Tong Zhao, Yong-Qi Zhao, Ming Fan, Hai-Tao Wu and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
12.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

64 citing papers in PubMed, 88 citations in OpenAlex.

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4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 1 country.

Yun-Ling He *Department of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.ORCID 0000-0003-1353-328X
Jian Li *State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing, 100850, China.ORCID 0000-0003-2131-321X
Sheng-Hui GongDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.
Xiang ChengDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.
Ming ZhaoDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.
Yan CaoState Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing, 100850, China.
Tong ZhaoDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.
Yong-Qi ZhaoDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China.
Ming FanDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China. fanmingchina@126.com.ORCID 0000-0002-2220-2231
Hai-Tao WuDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China. wuht@bmi.ac.cn.ORCID 0000-0001-8437-3194
Ling-Ling ZhuDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China. linglingzhu@hotmail.com.
Li-Ying WuDepartment of Neurobiology, Beijing Institute of Basic Medical Sciences, Beijing, 100850, China. liyingwu_china@163.com.ORCID 0000-0001-5277-2078
Beijing Institute of Education · CNCapital Medical University · CNBeijing Proteome Research Center · CNInstitute of Microbiology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitophagy is an important metabolic mechanism that modulates mitochondrial quality and quantity by selectively removing damaged or unwanted mitochondria. BNIP3 (BCL2/adenovirus e1B 19 kDa protein interacting protein 3), a mitochondrial outer membrane protein, is a mitophagy receptor that mediates mitophagy under various stresses, particularly hypoxia, since BNIP3 is a hypoxia-responsive protein. However, the underlying mechanisms that regulate BNIP3 and thus mediate mitophagy under hypoxic conditions remain elusive. Here, we demonstrate that in hypoxia JNK1/2 (c-Jun N-terminal kinase 1/2) phosphorylates BNIP3 at Ser 60/Thr 66, which hampers proteasomal degradation of BNIP3 and drives mitophagy by facilitating the direct binding of BNIP3 to LC3 (microtubule-associated protein 1 light chain 3), while PP1/2A (protein phosphatase 1/2A) represses mitophagy by dephosphorylating BNIP3 and triggering its proteasomal degradation. These findings reveal the intrinsic mechanisms cells use to regulate mitophagy via the JNK1/2-BNIP3 pathway in response to hypoxia. Thus, the JNK1/2-BNIP3 signaling pathway strongly links mitophagy to hypoxia and may be a promising therapeutic target for hypoxia-related diseases.

Indexed as

HypoxiaMitophagyHumansMembrane ProteinsMitochondriaMitochondrial MembranesMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9PhosphorylationProto-Oncogene ProteinsBNIP3 protein, humanMembrane ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Proto-Oncogene Proteins

Identifiers

PMID36396625
PMCPMC9672126
OpenAlexW4309235948

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.