Evidence map›Paper›PMID 24574454›Full record

ArticleMolecular biology of the cell2014

FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in Chlamydomonas.

Haru-aki Yanagisawa, Garrison Mathis, Toshiyuki Oda, Masafumi Hirono, Elizabeth A Richey, Hiroaki Ishikawa, Wallace F Marshall, Masahide Kikkawa, Hongmin Qin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.5field-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

49 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Microtubule inner proteins ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. FAP20 is required for flagellum assembly inMolecular biology of the cell · 2024
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  12. FAP20 is required for flagellum assembly inbioRxiv : the preprint server for biology · 2024
    Article
  13. Frontiers in cell and developmental biology · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Modulation of inner junction proteins contributes to axoneme differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
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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

9 authors at 3 institutions in 2 countries.

Haru-aki YanagisawaDepartment of Cell Biology and Anatomy, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan Department of Biological Sciences, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan Department of Biology, Texas A&M University, College Station, TX 77843 Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158.
Garrison Mathis
Toshiyuki Oda
Masafumi Hirono
Elizabeth A Richey
Hiroaki Ishikawa
Wallace F Marshall
Masahide Kikkawa
Hongmin Qin
The University of Tokyo · JPTexas A&M University · USUniversity of California, San Francisco · US

Funding

Modeling and Analysis of the Flagellar Length Control SystemR01GM097017 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MARSHALL, WALLACE · 2011 to 2018
$2.1M
NIGMS NIH HHS R01 GM097017
6 · The paper itself

Abstract

The axoneme-the conserved core of eukaryotic cilia and flagella-contains highly specialized doublet microtubules (DMTs). A long-standing question is what protein(s) compose the junctions between two tubules in DMT. Here we identify a highly conserved flagellar-associated protein (FAP), FAP20, as an inner junction (IJ) component. The flagella of Chlamydomonas FAP20 mutants have normal length but beat with an abnormal symmetrical three-dimensional pattern. In addition, the mutant axonemes are liable to disintegrate during beating, implying that interdoublet connections may be weakened. Conventional electron microscopy shows that the mutant axonemes lack the IJ, and cryo-electron tomography combined with a structural labeling method reveals that the labeled FAP20 localizes at the IJ. The mutant axonemes also lack doublet-specific beak structures, which are localized in the proximal portion of the axoneme and may be involved in planar asymmetric flagellar bending. FAP20 itself, however, may not be a beak component, because uniform localization of FAP20 along the entire length of all nine DMTs is inconsistent with the beak's localization. FAP20 is the first confirmed component of the IJ. Our data also suggest that the IJ is important for both stabilizing the axoneme and scaffolding intra-B-tubular substructures required for a planar asymmetrical waveform.

Indexed as

AnimalsAxonemeChlamydomonas reinhardtiiFlagellaMicrotubulesPlant ProteinsProtein StabilityProtein TransportZebrafishPlant Proteins

Identifiers

PMID24574454
PMCPMC4004596
OpenAlexW2012973861

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.