Evidence map›Paper›PMID 33397950›Full record

ArticleNature communications2021

Metaxins are core components of mitochondrial transport adaptor complexes.

Yinsuo Zhao, Eli Song, Wenjuan Wang, Chung-Han Hsieh, Xinnan Wang, Wei Feng, Xiangming Wang, Kang Shen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 93 citations in OpenAlex.

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  10. Kinesins inOpen biology · 2025
    Review
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  13. Molecular mechanisms of mitochondrial quality control.Translational neurodegeneration · 2025
    Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

2 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

8 authors at 4 institutions in 2 countries.

Yinsuo ZhaoNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.
Eli SongNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.ORCID 0000-0002-7546-5609
Wenjuan WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China.
Chung-Han HsiehDepartment of Neurosurgery, Stanford University School of Medicine, Stanford, CA, Stanford, CA, USA.
Xinnan WangDepartment of Neurosurgery, Stanford University School of Medicine, Stanford, CA, Stanford, CA, USA.ORCID 0000-0002-2640-7082
Wei FengNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China. wfeng@ibp.ac.cn.ORCID 0000-0001-9738-9398
Xiangming WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, 100101, China. xmwang@ibp.ac.cn.
Kang ShenHoward Hughes Medical Institute, Department of Biology, Stanford University, Stanford, CA, USA. kangshen@stanford.edu.ORCID 0000-0003-4059-8249
Chinese Academy of Sciences · CNInstitute of Biophysics · CNHoward Hughes Medical Institute · USStanford University · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Trafficking of mitochondria into dendrites and axons plays an important role in the physiology and pathophysiology of neurons. Mitochondrial outer membrane protein Miro and adaptor proteins TRAKs/Milton link mitochondria to molecular motors. Here we show that metaxins MTX-1 and MTX-2 contribute to mitochondrial transport into both dendrites and axons of C. elegans neurons. MTX1/2 bind to MIRO-1 and kinesin light chain KLC-1, forming a complex to mediate kinesin-1-based movement of mitochondria, in which MTX-1/2 are essential and MIRO-1 plays an accessory role. We find that MTX-2, MIRO-1, and TRAK-1 form another distinct adaptor complex to mediate dynein-based transport. Additionally, we show that failure of mitochondrial trafficking in dendrites causes age-dependent dendrite degeneration. We propose that MTX-2 and MIRO-1 form the adaptor core for both motors, while MTX-1 and TRAK-1 specify each complex for kinesin-1 and dynein, respectively. MTX-1 and MTX-2 are also required for mitochondrial transport in human neurons, indicative of their evolutionarily conserved function.

Indexed as

AnimalsAnimals, Genetically ModifiedAxonsCaenorhabditis elegans ProteinsDendritesGreen Fluorescent ProteinsHEK293 CellsHumansKinesinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsProtein BindingProtein TransportCaenorhabditis elegans ProteinsGreen Fluorescent ProteinsKinesinsKLC1 protein, humanMitochondrial Membrane Transport ProteinsMitochondrial Proteinsmtx-1 protein, C elegansmtx-2 protein, C elegans

Identifiers

PMID33397950
PMCPMC7782850
OpenAlexW3119137463

What OpenQuestion 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 OpenQuestion graph.