Evidence map›Paper›PMID 20829795›Full record

ArticleNature2010

MEC-17 is an alpha-tubulin acetyltransferase.

Jyothi S Akella, Dorota Wloga, Jihyun Kim, Natalia G Starostina, Sally Lyons-Abbott, Naomi S Morrissette, Scott T Dougan, Edward T Kipreos, Jacek Gaertig

Open access · greenAbstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 279 papers.

0numbers the graph read from it
0cells of the map it votes in
279citing papers in PubMed
12.9field-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

279 citing papers in PubMed, 473 citations in OpenAlex.

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  16. Cytomegalovirus disrupts Lamin A/C to control microtubule-mediated nuclear movement and cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2025
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219 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

9 authors at 2 institutions in 1 country.

Jyothi S AkellaDepartment of Cellular Biology, University of Georgia, Athens, Georgia 30602, USA.
Dorota Wloga
Jihyun Kim
Natalia G Starostina
Sally Lyons-Abbott
Naomi S Morrissette
Scott T Dougan
Edward T Kipreos
Jacek Gaertig
University of Georgia · USUniversity of California, Irvine · US

Funding

Regulation of the cell cycle and signaling by CUL-2 E3 complexesR01GM074212 · NIGMS · UNIVERSITY OF GEORGIA · PI KIPREOS, EDWARD T. · 2007 to 2015
$2.3M
Mechanisms of Dinitroaniline Action, Selectivity and ResistanceR01AI067981 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI MORRISSETTE, NAOMI S · 2006 to 2010
$1.7M
Functional Adaptation of Microtubules by AcetylationR01GM089912 · NIGMS · UNIVERSITY OF GEORGIA · PI GAERTIG, JACEK · 2010 to 2013
$1.1M
NIAID NIH HHS R01 AI067981NIAID NIH HHS R01AI067981NIGMS NIH HHS R01 GM074212NIGMS NIH HHS R01GM074212NIGMS NIH HHS R01 GM089912NIGMS NIH HHS R01GM089912
6 · The paper itself

Abstract

In most eukaryotic cells, subsets of microtubules are adapted for specific functions by post-translational modifications (PTMs) of tubulin subunits. Acetylation of the epsilon-amino group of K40 on alpha-tubulin is a conserved PTM on the luminal side of microtubules that was discovered in the flagella of Chlamydomonas reinhardtii. Studies on the significance of microtubule acetylation have been limited by the undefined status of the alpha-tubulin acetyltransferase. Here we show that MEC-17, a protein related to the Gcn5 histone acetyltransferases and required for the function of touch receptor neurons in Caenorhabditis elegans, acts as a K40-specific acetyltransferase for alpha-tubulin. In vitro, MEC-17 exclusively acetylates K40 of alpha-tubulin. Disruption of the Tetrahymena MEC-17 gene phenocopies the K40R alpha-tubulin mutation and makes microtubules more labile. Depletion of MEC-17 in zebrafish produces phenotypes consistent with neuromuscular defects. In C. elegans, MEC-17 and its paralogue W06B11.1 are redundantly required for acetylation of MEC-12 alpha-tubulin, and contribute to the function of touch receptor neurons partly via MEC-12 acetylation and partly via another function, possibly by acetylating another protein. In summary, we identify MEC-17 as an enzyme that acetylates the K40 residue of alpha-tubulin, the only PTM known to occur on the luminal surface of microtubules.

Indexed as

AcetylationAcetyltransferasesAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell LineDipodomysHumansProtozoan ProteinsTetrahymenaTouchTubulinZebrafishZebrafish ProteinsAcetyltransferasesalpha-tubulin acetylaseatat1 protein, zebrafishCaenorhabditis elegans ProteinsMEC-17 protein, C elegansProtozoan ProteinsTubulinZebrafish Proteins

Identifiers

PMID20829795
PMCPMC2938957
OpenAlexW1585324347

What OpenQuestion holds

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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.