Evidence map›Paper›PMID 24520046›Full record

ArticleCytoskeleton (Hoboken, N.J.)2014

Tau interconverts between diffusive and stable populations on the microtubule surface in an isoform and lattice specific manner.

Derrick P McVicker, Gregory J Hoeprich, Andrew R Thompson, Christopher L Berger

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  4. Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Article
  7. The pathogenic R5L mutation disrupts formation of Tau complexes on the microtubule by altering local N-terminal structure.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Tau Isoforms Imbalance Impairs the Axonal Transport of the Amyloid Precursor Protein in Human Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  16. Article
  17. The Dark Matter of Biology.Biophysical journal · 2016
    Review
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Derrick P McVickerCell and Molecular Biology Program, University of Vermont College of Medicine, Burlington, Vermont.
Gregory J Hoeprich
Andrew R Thompson
Christopher L Berger
University of Vermont · US

Funding

Tau-mediated regulation of axonal transportR01GM101066 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI BERGER, CHRISTOPHER L. · 2013 to 2016
$1.6M
NIGMS NIH HHS R01 GM101066
6 · The paper itself

Abstract

It has been demonstrated that Tau exists on the microtubule lattice in both diffusing and static populations, but how this may relate to Tau function is currently unclear. Tau isoforms are developmentally regulated and have been shown to have disparate effects on microtubule polymerization, the ability to bind microtubules, and the ability to inhibit kinesin. It has also been shown that Tau is sensitive to microtubule stabilizing agents and the ability to affect the persistence length of microtubules and to inhibit kinesin can be altered by stabilizing microtubules with various nucleotide analogs. Given these observations, it is likely the behavior of Tau is dictated by both the isoform of Tau and by structural changes in the microtubule lattice. In the present study, we use single molecule imaging to examine the behavior of the three-repeat short (3RS) isoform and the four-repeat long (4RL) isoform on different microtubule tracks stabilized with either paclitaxel or guanylyl-(α,β)-methylene-diphosphate (GMPCPP). On paclitaxel-stabilized microtubules, we find 3RS-Tau favors the static conformation and forms complexes consisting of 2-3 molecules, while 4RL-Tau predominantly exists as a single molecule equally distributed between the static and diffusing populations. However, on GMPCPP-stabilized microtubules both isoforms favor the diffusing conformation and do not form static complexes composed of more than one Tau molecule. We find both isoforms of Tau interconvert between static and diffusing populations on the microtubule surface, and the equilibrium between these two states depends on both the isoform of Tau and the structure of the underlying microtubule lattice.

Indexed as

AnimalsCattleDiffusionGuanosine TriphosphateHumansKymographyMicrotubulesPaclitaxelProtein Isoformstau ProteinsTime Factors5'-guanylylmethylenebisphosphonateGuanosine TriphosphatePaclitaxelProtein Isoformstau ProteinscytoskeletonkinesinmicrotubuleneuronnucleotideTau

Identifiers

PMID24520046
PMCPMC4154625
OpenAlexW1829764368

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.