Evidence map›Paper›PMID 25658008›Full record

ArticleBiophysical journal2014

The motility of axonemal dynein is regulated by the tubulin code.

Joshua D Alper, Franziska Decker, Bernice Agana, Jonathon Howard

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

42 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Review
  3. Acetylation and Deacetylation of Cytoskeleton-Associated Proteins.Results and problems in cell differentiation · 2025
    Review
  4. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  5. Article
  6. Article
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  8. Article
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  12. Article
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  15. Article
  16. Article
  17. Review
  18. Review
  19. Cilia, neural development and disease.Seminars in cell & developmental biology · 2021
    Review
  20. Review
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

4 authors at 2 institutions in 2 countries.

Joshua D AlperDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Franziska DeckerMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Bernice AganaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Jonathon HowardDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. Electronic address: jonathon.howard@yale.edu.
Max Planck Institute of Molecular Cell Biology and Genetics · DEYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule diversity, arising from the utilization of different tubulin genes and from posttranslational modifications, regulates many cellular processes including cell division, neuronal differentiation and growth, and centriole assembly. In the case of cilia and flagella, multiple cell biological studies show that microtubule diversity is important for axonemal assembly and motility. However, it is not known whether microtubule diversity directly influences the activity of the axonemal dyneins, the motors that drive the beating of the axoneme, nor whether the effects on motility are indirect, perhaps through regulatory pathways upstream of the motors, such as the central pair, radial spokes, or dynein regulatory complex. To test whether microtubule diversity can directly regulate the activity of axonemal dyneins, we asked whether in vitro acetylation or deacetylation of lysine 40 (K40), a major posttranslational modification of α-tubulin, or whether proteolytic cleavage of the C-terminal tail (CTT) of α- and β-tubulin, the location of detyrosination, polyglutamylation, and polyglycylation modifications as well as most of the genetic diversity, can influence the activity of outer arm axonemal dynein in motility assays using purified proteins. By quantifying the motility with displacement-weighted velocity analysis and mathematically modeling the results, we found that K40 acetylation increases and CTTs decrease axonemal dynein motility. These results show that axonemal dynein directly deciphers the tubulin code, which has important implications for eukaryotic ciliary beat regulation.

Indexed as

Protein Processing, Post-TranslationalAcetylationAxonemal DyneinsChlamydomonas reinhardtiiModels, BiologicalMotionProteolysisTubulinAxonemal DyneinsTubulin

Identifiers

PMID25658008
PMCPMC4808650
OpenAlexW2028880470

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.