Evidence map›Paper›PMID 21262966›Full record

ArticleThe Journal of biological chemistry2011

Tubulin tyrosine ligase-like genes ttll3 and ttll6 maintain zebrafish cilia structure and motility.

Narendra Pathak, Christina A Austin, Iain A Drummond

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
3.4field-weighted citation impact, top 8% 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, 114 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Post-Translational Modifications in Cilia and Ciliopathies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Ttc30a affects tubulin modifications in a model for ciliary chondrodysplasia with polycystic kidney disease.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Review

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

3 authors at 1 institution in 1 country.

Narendra PathakNephrology Division, Massachusetts General Hospital, Charlestown, Massachusetts 02129, USA.
Christina A Austin
Iain A Drummond
Harvard University · US

Funding

GENETIC ANALYSIS OF ZEBRAFISH KIDNEY DEVELOPMENTR01DK053093 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI DRUMMOND, IAIN A. · 1997 to 2018
$5.2M
Polycystin function in zebrafish (PA-06-158)R01DK070263 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI DRUMMOND, IAIN A. · 2004 to 2014
$2.9M
Fleer: Functional study in regulation of vertebrate cilia tublin modificationK01DK078741 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI PATHAK, NARENDRA H · 2008 to 2012
$687k
NIDDK NIH HHS K01 DK078741NIDDK NIH HHS K01DK078741NIDDK NIH HHS R01 DK053093NIDDK NIH HHS R01DK053093NIDDK NIH HHS R01 DK070263
6 · The paper itself

Abstract

Tubulin post-translational modifications generate microtubule heterogeneity and modulate microtubule function, and are catalyzed by tubulin tyrosine ligase-like (TTLL) proteins. Using antibodies specific to monoglycylated, polyglycylated, and glutamylated tubulin in whole mount immunostaining of zebrafish embryos, we observed distinct, tissue-specific patterns of tubulin modifications. Tubulin modification patterns in cilia correlated with the expression of ttll3 and ttll6 in ciliated cells. Expression screening of all zebrafish tubulin tyrosine ligase-like genes revealed additional tissue-specific expression of ttll1 in brain neurons, ttll4 in muscle, and ttll7 in otic placodes. Knockdown of ttll3 eliminated cilia tubulin glycylation but had surprisingly mild effects on cilia structure and motility. Similarly, knockdown of ttll6 strongly reduced cilia tubulin glutamylation but only partially affected cilia structure and motility. Combined loss of function of ttll3 and ttll6 caused near complete loss of cilia motility and induced a variety of axonemal ultrastructural defects similar to defects previously observed in zebrafish fleer mutants, which were shown to lack tubulin glutamylation. Consistently, we find that fleer mutants also lack tubulin glycylation. These results indicate that tubulin glycylation and glutamylation have overlapping functions in maintaining cilia structure and motility and that the fleer/dyf-1 TPR protein is required for both types of tubulin post-translational modification.

Indexed as

AnimalsAxonemeCiliaGene Expression Regulation, EnzymologicGene Knockdown TechniquesMutationOrgan SpecificityPeptide SynthasesProtein Processing, Post-TranslationalTubulinZebrafishZebrafish Proteinsflr protein, zebrafishPeptide SynthasesTtll3 protein, zebrafishTubulintubulin polyglutamylaseZebrafish Proteins

Identifiers

PMID21262966
PMCPMC3064220
OpenAlexW2013469097

What OpenQuestion holds

Textmetadata
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.