Evidence map›Paper›PMID 30404948›Full record

ArticleThe Journal of cell biology2019

FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function.

Liang Wang, Ziyi Yan, Helena Vihinen, Ove Eriksson, Weihuan Wang, Rabah Soliymani, Yao Lu, Yaxin Xue, Eija Jokitalo, Jing Li and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

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  16. Mitochondrial Membrane Remodeling.Frontiers in bioengineering and biotechnology · 2021
    Review
  17. Article
  18. Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020
    Review
  19. The cell biology of mitochondrial membrane dynamics.Nature reviews. Molecular cell biology · 2020
    Review
  20. Article
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

11 authors at 2 institutions in 2 countries.

Liang WangInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Ziyi YanInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-6598-4085
Helena VihinenInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-3862-9237
Ove ErikssonBiochemistry/Developmental Biology, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-3565-4106
Weihuan WangInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Rabah SoliymaniMeilahti Clinical Proteomics Core Facility, HiLIFE, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Yao LuInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Yaxin XueInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.
Eija JokitaloInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-4159-6934
Jing LiCollege of Life Sciences, Northwest A&F University, Yangling, China.
Hongxia ZhaoInstitute of Biotechnology, University of Helsinki, Helsinki, Finland hongxia.zhao@helsinki.fi.ORCID 0000-0002-1606-5621
University of Helsinki · FINorthwest A&F University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.

Indexed as

Cell Line, TumorCell ProliferationElectron Transport Chain Complex ProteinsGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsHumansMembrane Transport ProteinsMicroscopy, FluorescenceMitochondriaMitochondrial MembranesMitochondrial Precursor Protein Import Complex ProteinsMitochondrial Proton-Translocating ATPasesOsteoblastsOxidative PhosphorylationProtein DomainsCIBAR1 protein, humanElectron Transport Chain Complex ProteinsGreen Fluorescent ProteinsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial Proton-Translocating ATPasesProteinsReceptors, Cell SurfaceRNA, Small InterferingTOMM20 protein, human

Identifiers

PMID30404948
PMCPMC6314547
OpenAlexW2899882305

What Socratic holds

Textmetadata
LicenceCC BY-NC-SA
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.