Evidence map›Paper›PMID 1740474›Full record

ArticleThe Journal of cell biology1992

The plus ends of stable microtubules are the exclusive nucleating structures for microtubules in the axon.

P W Baas, F J Ahmad

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 114 citations in OpenAlex.

  1. Patient-derived forebrain cortical organoids reveal biphasic tau-MAP6-microtubule axis dysfunction in tauopathy.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  2. Regulation of Axonal Microtubule Polarity Orientation in Different Kinds of Neurons.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  3. Review
  4. Article
  5. Article
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  7. Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Article
  10. Review
  11. Stability properties of neuronal microtubules.Cytoskeleton (Hoboken, N.J.) · 2016
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Uniform polarity microtubule assemblies imaged in native brain tissue by second-harmonic generation microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  17. Visualization of microtubule growth in cultured neurons via the use of EB3-GFP (end-binding protein 3-green fluorescent protein).The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  18. Reorganization and movement of microtubules in axonal growth cones and developing interstitial branches.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

P W BaasDepartment of Anatomy, University of Wisconsin Medical School, Madison 53706.
F J Ahmad
University of Wisconsin System · US

Funding

MICROTUBULE DYNAMICS AND AXON GROWTHR01NS028785 · NINDS · UNIVERSITY OF WISCONSIN MADISON · PI BAAS, PETER W. · 1990 to 2021
$7.3M
Microtubule Dynamics and Axon GrowthR56NS028785 · NINDS · DREXEL UNIVERSITY · PI BAAS, PETER W. · 2012 to 2012
$384k
NINDS NIH HHS NS 28785
6 · The paper itself

Abstract

Microtubules (MTs) in the axon have a uniform polarity orientation that is recapitulated during recovery from episodes of MT depolymerization (Heidemann, S. R., M. A. Hamborg, S. J. Thomas, B. Song, S. Lindley, and D. Chu. 1984. J. Cell Biol. 99:1289-1295). This tight regulation of their organization indicates that axonal MTs are spatially regulated by discrete nucleating structures comparable in function to the centrosome. Several authors have proposed that an especially stable class of MTs in the axon may serve as these nucleating structures. In a previous report (Baas, P. W., and M. M. Black. 1990. J. Cell Biol. 111:495-509), we determined that the axons of cultured sympathetic neurons contain two classes of MT polymer, stable and labile, that differ in their sensitivity to nocodazole by roughly 35-fold. The stable and labile polymer represent long-lived and recently assembled polymer, respectively. We also determined that these two classes of polymer can be visually distinguished at the immunoelectron microscopic level based on their content of tyrosinated alpha-tubulin: the labile polymer stains densely, while the stable polymer does not stain. In the present study, we have taken advantage of these observations to directly identify MT nucleating structures in the axon. Neuron cultures were treated with nocodazole for 6 h to completely depolymerize the labile polymer in the axon, and substantially shorten the stable polymer. The cultures were then rinsed free of the drug, permitted to reassemble polymer for various periods of time, and prepared for immunoelectron microscopic localization of tyrosinated alpha-tubulin. Serial reconstruction of consecutive thin sections was undertaken to determine the spatial relationship between the stable MTs and the newly assembled polymer. All of the new polymer assembled in direct continuity with the plus ends of stable MTs, indicating that these ends are assembly competent, and hence capable of acting as nucleating structures. Our results further indicate that no self-assembly of MTs occurs in the axon, nor do any MT nucleating structures exist in the axon other than the plus ends of stable MTs. Thus the plus ends of stable MTs are the exclusive nucleating structures for MTs in the axon.

Indexed as

AnimalsAnimals, NewbornAxonsCell PolarityCells, CulturedGanglia, SympatheticMicrotubule ProteinsMicrotubulesMolecular StructureNocodazoleRatsTubulinTyrosineMicrotubule ProteinsNocodazoleTubulinTyrosine

Identifiers

PMID1740474
PMCPMC2289361
OpenAlexW2117972095

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.