Evidence map›Paper›PMID 8795628›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1996

A spatial gradient of tau protein phosphorylation in nascent axons.

J W Mandell, G A Banker

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

100 citing papers in PubMed, 267 citations in OpenAlex.

  1. Review
  2. MTCL2 Is Essential for the Bipolar-to-Multipolar Transition in the Dendrite Extension of Cerebellar Granule Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
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  4. Review
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  13. Review
  14. Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies.International journal of molecular sciences · 2020
    Review

40 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

2 authors at 1 institution in 1 country.

J W MandellDepartment of Neuroscience, University of Virginia School of Medicine, Charlottesville 22908, USA.
G A Banker
University of Virginia · US

Funding

THE DEVELOPMENT OF HIPPOCAMPAL NEURONS IN CULTURER01NS017112 · NINDS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI BANKER, GARY A · 1985 to 2008
$2.6M
NINDS NIH HHS NS09491NINDS NIH HHS NS17112NINDS NIH HHS R01 NS017112
6 · The paper itself

Abstract

Mechanisms underlying axonogenesis remain obscure. Although a large number of proteins eventually become polarized to the axonal domain, in no case does protein compartmentalization occur before or simultaneous with the earliest morphological expression of axonal properties. How then might initially unpolarized proteins, such as the microtubule-associated protein tau, play a role in the microdifferentiation of axons? We hypothesized that tau function could be locally regulated by phosphorylation during the period of axonogenesis. To test this hypothesis, we mapped relative levels of tau phosphorylation within developing cultured hippocampal neurons. This was accomplished using calibrated immunofluorescence ratio measurements employing phosphorylation state-dependent and state-independent antibodies. Tau in the nascent axon is more highly dephosphorylated at the site recognized by the tau-1 antibody than tau in the somatodendritic compartment. The change in phosphorylation state from soma to axon takes the form of a smooth proximo-distal gradient, with tau in the soma, immature dendrites and proximal axon approximately 80% phosphorylated at the tau-1 site, and that in the axonal growth cone only 20% phosphorylated. The existence of real spatial differences in tau phosphorylation state was confirmed by in situ phosphatase and kinase treatment. Pervanadate, a tyrosine phosphatase inhibitor, induced rapid tau dephosphorylation within live cells, effectively abolishing the phosphorylation gradient. Thus, the gradient is dynamic and potentially regulatable by upstream signals involving tyrosine phosphorylation. Phosphorylation gradients are likely to be present on many neuronal proteins in addition to tau, and their modulation by transmembrane signals could direct the establishment of polarity.

Indexed as

AnimalsAxonsCalibrationCells, CulturedEpitopesFluorescent Antibody TechniqueHippocampusImmunoblottingMicroscopy, FluorescenceNeuronsPhosphorylationProtein Tyrosine PhosphatasesRatstau ProteinsTissue DistributionVanadatesEpitopespervanadateProtein Tyrosine Phosphatasestau ProteinsVanadates

Identifiers

PMID8795628
PMCPMC6578967
OpenAlexW2138070279

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.