Evidence map›Paper›PMID 22658592›Full record

ArticleCurrent biology : CB2012

Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubules.

Juan G Cueva, Jen Hsin, Kerwyn Casey Huang, Miriam B Goodman

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
8.4field-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

109 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
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  4. Review
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  8. Article
  9. The alpha tubulin acetyltransferasemicroPublication biology · 2025
    Article
  10. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Native molecular architectures of centrosomes inbioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Juan G CuevaDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.
Jen Hsin
Kerwyn Casey Huang
Miriam B Goodman
Stanford University · US

Funding

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
Engineering of cell shape and intracellular organizationDP2OD006466 · OD · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 2009 to 2009
$2.4M
NIBIB NIH HHS R01 EB006745NIBIB NIH HHS R01EB006745NIH HHS DP2 OD006466NIH HHS DP2OD006466NINDS NIH HHS R01 NS047715NINDS NIH HHS R01NS047715
6 · The paper itself

Abstract

backgroundMicrotubules are built from linear polymers of α-β tubulin dimers (protofilaments) that form a tubular quinary structure. Microtubules assembled from purified tubulin in vitro contain between 10 and 16 protofilaments; however, such structural polymorphisms are not found in cells. This discrepancy implies that factors other than tubulin constrain microtubule protofilament number, but the nature of these constraints is unknown.

resultsHere, we show that acetylation of MEC-12 α-tubulin constrains protofilament number in C. elegans touch receptor neurons (TRNs). Whereas the sensory dendrite of wild-type TRNs is packed with a cross-linked bundle of long, 15-protofilament microtubules, mec-17;atat-2 mutants lacking α-tubulin acetyltransferase activity have short microtubules, rampant lattice defects, and variable protofilament number both between and within microtubules. All-atom molecular dynamics simulations suggest a model in which acetylation of lysine 40 promotes the formation of interprotofilament salt bridges, stabilizing lateral interactions between protofilaments and constraining quinary structure to produce stable, structurally uniform microtubules in vivo.

conclusionsAcetylation of α-tubulin is an essential constraint on protofilament number in vivo. We propose a structural model in which this posttranslational modification promotes the formation of lateral salt bridges that fine-tune the association between adjacent protofilaments and enable the formation of uniform microtubule populations in vivo.

Indexed as

Models, MolecularAcetylationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsMechanoreceptorsMicroscopy, ElectronMicrotubulesMolecular Dynamics SimulationProtein Processing, Post-TranslationalTubulinCaenorhabditis elegans ProteinsMEC-12 protein, C elegansTubulin

Identifiers

PMID22658592
PMCPMC3670109
OpenAlexW2050148731

What OpenQuestion holds

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LicenceTDM
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.