Evidence map›Paper›PMID 21068373›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation.

Toshinobu Shida, Juan G Cueva, Zhenjie Xu, Miriam B Goodman, Maxence V Nachury

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 281 papers.

0numbers the graph read from it
0cells of the map it votes in
281citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

281 citing papers in PubMed, 458 citations in OpenAlex.

  1. Article
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  5. PMEnvironment & health (Washington, D.C.) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. An Orthogonal Way of Writing the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026
    Review
  13. Togaram Ensures Axial Alignment of the Sperm Neck.bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Microtubule inner proteins in apicomplexan parasites.Biochemical Society transactions · 2026
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

221 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Toshinobu ShidaDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5345, USA.
Juan G Cueva
Zhenjie Xu
Miriam B Goodman
Maxence V Nachury
Kettering University · USStanford University · US

Funding

Quality control of the primary cilium proteomeR01GM089933 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Maxence V Nachury · 2010 to 2026
$5.8M
Molecular Basis of Sensory Transduction in C. elegansR01NS047715 · NINDS · STANFORD UNIVERSITY · PI GOODMAN, MIRIAM B · 2004 to 2017
$4.9M
Force Clamp Systems for Evaluation of MechanotransductionR01EB006745 · NIBIB · STANFORD UNIVERSITY · PI GOODMAN, MIRIAM B, PRUITT, BETH L · 2007 to 2014
$3.1M
NIBIB NIH HHS EB006745NIBIB NIH HHS R01 EB006745NIGMS NIH HHS GM089933NIGMS NIH HHS R01 GM089933NINDS NIH HHS NS047715NINDS NIH HHS R01 NS047715
6 · The paper itself

Abstract

Long-lived microtubules found in ciliary axonemes, neuronal processes, and migrating cells are marked by α-tubulin acetylation on lysine 40, a modification that takes place inside the microtubule lumen. The physiological importance of microtubule acetylation remains elusive. Here, we identify a BBSome-associated protein that we name αTAT1, with a highly specific α-tubulin K40 acetyltransferase activity and a catalytic preference for microtubules over free tubulin. In mammalian cells, the catalytic activity of αTAT1 is necessary and sufficient for α-tubulin K40 acetylation. Remarkably, αTAT1 is universally and exclusively conserved in ciliated organisms, and is required for the acetylation of axonemal microtubules and for the normal kinetics of primary cilium assembly. In Caenorhabditis elegans, microtubule acetylation is most prominent in touch receptor neurons (TRNs) and MEC-17, a homolog of αTAT1, and its paralog αTAT-2 are required for α-tubulin acetylation and for two distinct types of touch sensation. Furthermore, in animals lacking MEC-17, αTAT-2, and the sole C. elegans K40α-tubulin MEC-12, touch sensation can be restored by expression of an acetyl-mimic MEC-12[K40Q]. We conclude that αTAT1 is the major and possibly the sole α-tubulin K40 acetyltransferase in mammals and nematodes, and that tubulin acetylation plays a conserved role in several microtubule-based processes.

Indexed as

AcetyltransferasesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCiliaMechanotransduction, CellularMicrotubulesSensory Receptor CellsSubstrate SpecificityTouchTubulinAcetyltransferasesalpha-tubulin acetylaseCaenorhabditis elegans ProteinsTubulin

Identifiers

PMID21068373
PMCPMC3003046
OpenAlexW1984167248

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.