Evidence map›Paper›PMID 34033790›Full record

ReviewCurrent biology : CB2021

Molecular mechanisms underlying microtubule growth dynamics.

Joseph M Cleary, William O Hancock

Open access · bronzeAbstract readReview
In one paragraph

Review in Current biology : CB, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
6.3field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 82 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. CLASP2 promotes repair of kinesin-1 damage to the microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  4. PMEnvironment & health (Washington, D.C.) · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025
    Article
  14. Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025
    Review
  15. Article
  16. Review
  17. Review
  18. 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.

Joseph M ClearyDepartment of Biomedical Engineering, Pennsylvania State University, University Park, PA 16802, USA.
William O HancockDepartment of Biomedical Engineering, Pennsylvania State University, University Park, PA 16802, USA. Electronic address: woh1@psu.edu.
Pennsylvania State University · US

Funding

Molecular mechanism of bidirectional transportR35GM139568 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI William Olaf Hancock · 2021 to 2026
$4.9M
Research Training in Physiological Adaptations to StressT32GM108563 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI CANTORNA, MARGHERITA T, KORZICK, DONNA HOPE · 2014 to 2023
$2.2M
Multimotor Mechanisms in Microtubule-based TransportR01GM121679 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI HANCOCK, WILLIAM OLAF · 2017 to 2020
$1.3M
Single-molecule interrogation of microtubule dynamics mechanismsR01GM135565 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICE, LUKE W · 2020 to 2023
$1.3M
NIGMS NIH HHS R01 GM121679NIGMS NIH HHS R01 GM135565NIGMS NIH HHS R35 GM139568NIGMS NIH HHS T32 GM108563
6 · The paper itself

Abstract

Microtubules are dynamic cytoskeletal filaments composed of αβ-tubulin heterodimers. Historically, the dynamics of single tubulin interactions at the growing microtubule tip have been inferred from steady-state growth kinetics. However, recent advances in the production of recombinant tubulin and in high-resolution optical and cryo-electron microscopies have opened new windows into understanding the impacts of specific intermolecular interactions during growth. The microtubule lattice is held together by lateral and longitudinal tubulin-tubulin interactions, and these interactions are in turn regulated by the GTP hydrolysis state of the tubulin heterodimer. Furthermore, tubulin can exist in either an extended or a compacted state in the lattice. Growing evidence has led to the suggestion that binding of microtubule-associated proteins (MAPs) or motors can induce changes in tubulin conformation and that this information can be communicated through the microtubule lattice. Progress in understanding how dynamic tubulin-tubulin interactions control dynamic instability has benefitted from visualizing structures of growing microtubule plus ends and through stochastic biochemical models constrained by experimental data. Here, we review recent insights into the molecular basis of microtubule growth and discuss how MAPs and regulatory proteins alter tubulin-tubulin interactions to exert their effects on microtubule growth and stability.

Indexed as

MicrotubulesTubulinCryoelectron MicroscopyGuanosine TriphosphateKineticsMicrotubule-Associated ProteinsGuanosine TriphosphateMicrotubule-Associated ProteinsTubulin

Identifiers

PMID34033790
PMCPMC8575376
OpenAlexW3165382431

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.