Evidence map›Paper›PMID 38177312›Full record

ArticleThe EMBO journal2024

The ER membrane protein complex restricts mitophagy by controlling BNIP3 turnover.

Jose M Delgado, Logan Wallace Shepard, Sarah W Lamson, Samantha L Liu, Christopher J Shoemaker

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 15 citations in OpenAlex.

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  15. Coordinating BNIP3/NIX-mediated mitophagy in space and time.Biochemical Society transactions · 2024
    Review
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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

5 authors at 1 institution in 1 country.

Jose M DelgadoDepartment of Biochemistry and Cell Biology, Geisel School of Medicine, Dartmouth College, Hanover, NH, USA.ORCID http://orcid.org/0000-0003-1895-3099
Logan Wallace ShepardDepartment of Biochemistry and Cell Biology, Geisel School of Medicine, Dartmouth College, Hanover, NH, USA.
Sarah W LamsonDepartment of Biochemistry and Cell Biology, Geisel School of Medicine, Dartmouth College, Hanover, NH, USA.
Samantha L LiuDepartment of Biochemistry and Cell Biology, Geisel School of Medicine, Dartmouth College, Hanover, NH, USA.
Christopher J ShoemakerDepartment of Biochemistry and Cell Biology, Geisel School of Medicine, Dartmouth College, Hanover, NH, USA. Christopher.J.Shoemaker@Dartmouth.edu.ORCID http://orcid.org/0000-0003-2004-6340
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Fred W Kolling IV · 1985 to 2026
$91.3M
Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MIERKE, DALE F · 2016 to 2025
$25.9M
Molecular mechanisms governing selective autophagy in mammalian cellsR35GM142644 · NIGMS · DARTMOUTH COLLEGE · PI Christopher J Shoemaker · 2021 to 2026
$2.5M
Super-resolution spinning disk confocal microscope for Dartmouth Life SciencesS10OD032310 · OD · DARTMOUTH COLLEGE · PI AHMED, YASMATH · 2022 to 2022
$600k
Acquisition of the NextSeq2000 Sequencing platform to Increase Next Generation Sequencing Throughput While Reducing Costs at DartmouthS10OD030242 · OD · DARTMOUTH COLLEGE · PI KOLLING IV, FRED W · 2021 to 2021
$321k
Molecular Mechanisms of FUNDC1-Mediated MitophagyF31GM143849 · NIGMS · DARTMOUTH COLLEGE · PI DELGADO, JOSE M · 2022 to 2023
$90k
NCI NIH HHS P30 CA023108NIGMS NIH HHS F31 GM143849NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R35 GM142644NIH HHS S10 OD030242NIH HHS S10 OD032310
6 · The paper itself

Abstract

Lysosomal degradation of autophagy receptors is a common proxy for selective autophagy. However, we find that two established mitophagy receptors, BNIP3 and BNIP3L/NIX, are constitutively delivered to lysosomes in an autophagy-independent manner. This alternative lysosomal delivery of BNIP3 accounts for nearly all its lysosome-mediated degradation, even upon mitophagy induction. To identify how BNIP3, a tail-anchored protein in the outer mitochondrial membrane, is delivered to lysosomes, we performed a genome-wide CRISPR screen for factors influencing BNIP3 flux. This screen revealed both known modifiers of BNIP3 stability as well as a pronounced reliance on endolysosomal components, including the ER membrane protein complex (EMC). Importantly, the endolysosomal system and the ubiquitin-proteosome system regulated BNIP3 independently. Perturbation of either mechanism is sufficient to modulate BNIP3-associated mitophagy and affect underlying cellular physiology. More broadly, these findings extend recent models for tail-anchored protein quality control and install endosomal trafficking and lysosomal degradation in the canon of pathways that tightly regulate endogenous tail-anchored protein localization.

Indexed as

MitochondriaMitophagyAutophagyMembrane ProteinsMitochondrial MembranesMitochondrial ProteinsMembrane ProteinsMitochondrial ProteinsBNIP3EMCMitophagySecretory PathwayTA Protein

Identifiers

PMID38177312
PMCPMC10883272
OpenAlexW4390025629

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.