Evidence map›Paper›PMID 23583110›Full record

ArticleNeuron2013

Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules.

Yuyu Song, Laura L Kirkpatrick, Alexander B Schilling, Donald L Helseth, Nicolas Chabot, Jeffrey W Keillor, Gail V W Johnson, Scott T Brady

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
16.3field-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

107 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. The Lipotubuloids ofPlants (Basel, Switzerland) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025
    Review
  15. Article
  16. Article
  17. Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  18. Review
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Yuyu SongDepartment of Anatomy and Cell Biology, University of Illinois at Chicago, Chicago, IL 60612, USA.
Laura L Kirkpatrick
Alexander B Schilling
Donald L Helseth
Nicolas Chabot
Jeffrey W Keillor
Gail V W Johnson
Scott T Brady
University of Illinois Chicago · USUniversity of Ottawa · CALexicon Pharmaceuticals (United States) · USUniversity of Rochester Medical Center · US

Funding

MOLECULAR MECHANISMS OF AXONAL TRANSPORTR01NS023868 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1986 to 2010
$3.7M
PROPERTIES OF AXONAL TUBULIN RELATED TO NEURONAL GROWTHR01NS023320 · NINDS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BRADY, SCOTT THOMAS · 1985 to 2003
$1.0M
Molecular Mechanisms of Axonal TransportR56NS023868 · NINDS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BRADY, SCOTT THOMAS · 2011 to 2011
$554k
NINDS NIH HHS NS23320NINDS NIH HHS NS23868NINDS NIH HHS R01 NS023320NINDS NIH HHS R01 NS023868NINDS NIH HHS R56 NS023868
6 · The paper itself

Abstract

Neuronal microtubules support intracellular transport, facilitate axon growth, and form a basis for neuronal morphology. While microtubules in nonneuronal cells are depolymerized by cold, Ca(2+), or antimitotic drugs, neuronal microtubules are unusually stable. Such stability is important for normal axon growth and maintenance, while hyperstability may compromise neuronal function in aging and degeneration. Though mechanisms for stability are unclear, studies suggest that stable microtubules contain biochemically distinct tubulins that are more basic than conventional tubulins. Transglutaminase-catalyzed posttranslational incorporation of polyamines is one of the few modifications of intracellular proteins that add positive charges. Here we show that neuronal tubulin can be polyaminated by transglutaminase. Endogenous brain transglutaminase-catalyzed polyaminated tubulins have the biochemical characteristics of neuronal stable microtubules. Inhibiting polyamine synthesis or transglutaminase activity significantly decreases microtubule stability in vitro and in vivo. Together, these findings suggest that transglutaminase-catalyzed polyamination of tubulins stabilizes microtubules essential for unique neuronal structures and functions.

Indexed as

Protein Processing, Post-TranslationalAnimalsAxonsBrainCell FractionationCell Line, TransformedChromatography, High Pressure LiquidEnzyme InhibitorsGTP-Binding ProteinsMagnetic Resonance SpectroscopyMaleMiceMice, Inbred C57BLMice, KnockoutMicrotubulesModels, BiologicalEnzyme InhibitorsGTP-Binding ProteinsPolyaminesProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesTubulin

Identifiers

PMID23583110
PMCPMC3627183
OpenAlexW2044237166

What OpenQuestion holds

Textmetadata
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.