Evidence map›Paper›PMID 29849065›Full record

ArticleScientific reports2018

Environmental responsiveness of tubulin glutamylation in sensory cilia is regulated by the p38 MAPK pathway.

Yoshishige Kimura, Koji Tsutsumi, Alu Konno, Koji Ikegami, Saira Hameed, Tomomi Kaneko, Oktay Ismail Kaplan, Takayuki Teramoto, Manabi Fujiwara, Takeshi Ishihara and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Ciliary and Non-Ciliary Roles of IFT88 in Development and Diseases.International journal of molecular sciences · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Intraflagellar Transport Proteins as Regulators of Primary Cilia Length.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Review
  18. Functions of p38 MAP Kinases in the Central Nervous System.Frontiers in molecular neuroscience · 2020
    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

12 authors at 6 institutions in 4 countries.

Yoshishige KimuraDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan.
Koji TsutsumiDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan.
Alu KonnoDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan.
Koji IkegamiDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan.
Saira HameedDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan.
Tomomi KanekoDepartment of Liberal Arts and Sciences, Kanagawa University of Human Services, 1-10-1 Heisei-cho, Yokosuka, Kanagawa, 238-8522, Japan.
Oktay Ismail KaplanSchool of Biomolecular and Biomedical Science, University College Dublin, Belfield, Dublin, 4, Ireland.ORCID 0000-0002-8733-0920
Takayuki TeramotoDepartment of Biology, Faculty of Sciences, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan.
Manabi FujiwaraDepartment of Biology, Faculty of Sciences, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan.
Takeshi IshiharaDepartment of Biology, Faculty of Sciences, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka, 819-0395, Japan.
Oliver E BlacqueSchool of Biomolecular and Biomedical Science, University College Dublin, Belfield, Dublin, 4, Ireland.
Mitsutoshi SetouDepartment of Cellular & Molecular Anatomy, Hamamatsu University School of Medicine, 1-20-1 Handayama, Hamamatsu, Shizuoka, 431-3192, Japan. setou@hama-med.ac.jp.
Hamamatsu University School of Medicine · JPKyushu University · JPUniversity College Dublin · IEHamamatsu Photonics (Japan) · JPHiroshima University · JPKanagawa University of Human Services · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamylation is a post-translational modification found on tubulin that can alter the interaction between microtubules (MTs) and associated proteins. The molecular mechanisms regulating tubulin glutamylation in response to the environment are not well understood. Here, we show that in the sensory cilia of Caenorhabditis elegans, tubulin glutamylation is upregulated in response to various signals such as temperature, osmolality, and dietary conditions. Similarly, tubulin glutamylation is modified in mammalian photoreceptor cells following light adaptation. A tubulin glutamate ligase gene ttll-4, which is essential for tubulin glutamylation of axonemal MTs in sensory cilia, is activated by p38 MAPK. Amino acid substitution of TTLL-4 has revealed that a Thr residue (a putative MAPK-phosphorylation site) is required for enhancement of tubulin glutamylation. Intraflagellar transport (IFT), a bidirectional trafficking system specifically observed along axonemal MTs, is required for the formation, maintenance, and function of sensory cilia. Measurement of the velocity of IFT particles revealed that starvation accelerates IFT, which was also dependent on the Thr residue of TTLL-4. Similarly, starvation-induced attenuation of avoidance behaviour from high osmolality conditions was also dependent on ttll-4. Our data suggest that a novel evolutionarily conserved regulatory system exists for tubulin glutamylation in sensory cilia in response to the environment.

Indexed as

EnvironmentMAP Kinase Signaling SystemAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGlutamic AcidOlfactory Receptor Neuronsp38 Mitogen-Activated Protein KinasesPeptide SynthasesPhosphorylationProtein Processing, Post-TranslationalThreonineTubulinCaenorhabditis elegans ProteinsGlutamic Acidp38 Mitogen-Activated Protein KinasesPeptide SynthasesThreonineTTLL-4 protein, C elegansTubulin

Identifiers

PMID29849065
PMCPMC5976657
OpenAlexW2805536194

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.