Evidence map›Paper›PMID 23569216›Full record

ArticleThe Journal of cell biology2013

The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility.

Ryosuke Yamamoto, Kangkang Song, Haru-Aki Yanagisawa, Laura Fox, Toshiki Yagi, Maureen Wirschell, Masafumi Hirono, Ritsu Kamiya, Daniela Nicastro, Winfield S Sale

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

58 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. mSphere · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  15. PCD Genes-From Patients to Model Organisms and Back to Humans.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  18. Review
  19. Article
  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

10 authors at 3 institutions in 2 countries.

Ryosuke YamamotoDepartment of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Kangkang Song
Haru-Aki Yanagisawa
Laura Fox
Toshiki Yagi
Maureen Wirschell
Masafumi Hirono
Ritsu Kamiya
Daniela Nicastro
Winfield S Sale
Emory University · USThe University of Tokyo · JPBrandeis University · US

Funding

Structure and Function of Complexes that Regulate Ciliary MotilityR01GM083122 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Daniela Nicastro · 2007 to 2026
$6.2M
Functional Substructure of Flagellar DyneinR37GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 2002 to 2011
$4.0M
FUNCTIONAL SUBSTRUCTURE OF FLAGELLAR DYNEINR01GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 1994 to 2020
$3.6M
NIGMS NIH HHS GM051173NIGMS NIH HHS GM083122NIGMS NIH HHS R01 GM051173NIGMS NIH HHS R01 GM083122NIGMS NIH HHS R37 GM051173
6 · The paper itself

Abstract

Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo-electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin-dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility.

Indexed as

Cell MovementConserved SequenceAmino Acid SequenceAxonemeBase SequenceChlamydomonas reinhardtiiCiliaDyneinsGenes, PlantMicrotubulesModels, BiologicalModels, MolecularMolecular Sequence DataMultiprotein ComplexesMutationPhenotypeDyneinsMultiprotein ComplexesPlant ProteinsProtease Nexins

Identifiers

PMID23569216
PMCPMC3628515
OpenAlexW2119624567

What OpenQuestion 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 OpenQuestion graph.