Evidence map›Paper›PMID 27129203›Full record

ArticleThe Journal of biological chemistry2016

Structure and Dynamics of Single-isoform Recombinant Neuronal Human Tubulin.

Annapurna Vemu, Joseph Atherton, Jeffrey O Spector, Agnieszka Szyk, Carolyn A Moores, Antonina Roll-Mecak

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
10.8field-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

84 citing papers in PubMed, 133 citations in OpenAlex.

  1. Review
  2. Article
  3. Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Alpha-tubulin tails regulate axoneme differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  13. ProSComputational and structural biotechnology journal · 2025
    Article
  14. Article
  15. A Novel PathogenicGenes · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

24 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

6 authors at 3 institutions in 2 countries.

Annapurna VemuFrom the Cell Biology and Biophysics Unit, NINDS, and.
Joseph Athertonthe Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London WC1E, United Kingdom.
Jeffrey O SpectorFrom the Cell Biology and Biophysics Unit, NINDS, and.
Agnieszka SzykFrom the Cell Biology and Biophysics Unit, NINDS, and.
Carolyn A Mooresthe Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck College, University of London, London WC1E, United Kingdom c.moores@mail.cryst.bbk.ac.uk.
Antonina Roll-MecakFrom the Cell Biology and Biophysics Unit, NINDS, and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 and Antonina@mail.nih.gov.
National Institutes of Health · USInstitute of Structural and Molecular Biology · GBNational Institute of Neurological Disorders and Stroke · US

Funding

Readout of the tubulin code by cellular effectorsZIANS003164 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2017 to 2025
$11.7M
Mechanisms of molecular machines that regulate the neuronal cytoskeletonZIANS003122 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ROLL-MECAK, ANTONINA · 2010 to 2016
$9.9M
Intramural NIH HHS ZIA NS003122Medical Research Council MR/J000973/1
6 · The paper itself

Abstract

Microtubules are polymers that cycle stochastically between polymerization and depolymerization, i.e. they exhibit "dynamic instability." This behavior is crucial for cell division, motility, and differentiation. Although studies in the last decade have made fundamental breakthroughs in our understanding of how cellular effectors modulate microtubule dynamics, analysis of the relationship between tubulin sequence, structure, and dynamics has been held back by a lack of dynamics measurements with and structural characterization of homogeneous isotypically pure engineered tubulin. Here, we report for the first time the cryo-EM structure and in vitro dynamics parameters of recombinant isotypically pure human tubulin. α1A/βIII is a purely neuronal tubulin isoform. The 4.2-Å structure of post-translationally unmodified human α1A/βIII microtubules shows overall similarity to that of heterogeneous brain microtubules, but it is distinguished by subtle differences at polymerization interfaces, which are hot spots for sequence divergence between tubulin isoforms. In vitro dynamics assays show that, like mosaic brain microtubules, recombinant homogeneous microtubules undergo dynamic instability, but they polymerize slower and have fewer catastrophes. Interestingly, we find that epitaxial growth of α1A/βIII microtubules from heterogeneous brain seeds is inefficient but can be fully rescued by incorporating as little as 5% of brain tubulin into the homogeneous α1A/βIII lattice. Our study establishes a system to examine the structure and dynamics of mammalian microtubules with well defined tubulin species and is a first and necessary step toward uncovering how tubulin genetic and chemical diversity is exploited to modulate intrinsic microtubule dynamics.

Indexed as

AnimalsCryoelectron MicroscopyHumansMicrotubulesModels, MolecularNeuronsProtein IsoformsProtein MultimerizationProtein Structure, QuaternaryRecombinant ProteinsSf9 CellsSpodopteraTubulinProtein IsoformsRecombinant ProteinsTUBB3 protein, humanTubulincryo-electron microscopycryo-EMcytoskeletondynamic instabilityengineered tubulinmicroscopymicrotubulemicrotubule dynamicsmicrotubule structurepost-translational modificationrecombinant tubulintubulintubulin isoform

Identifiers

PMID27129203
PMCPMC4933209
OpenAlexW2344733175

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.