Evidence map›Paper›PMID 30837315›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Spastin is a dual-function enzyme that severs microtubules and promotes their regrowth to increase the number and mass of microtubules.

Yin-Wei Kuo, Olivier Trottier, Mohammed Mahamdeh, Jonathon Howard

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
6.7field-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

61 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. 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
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  9. Erk1Oncogene · 2025
    Article
  10. Article
  11. Article
  12. Unraveling Isoform Complexity: The Roles of M1- and M87-Spastin in Spastic Paraplegia 4 (SPG4).Movement disorders : official journal of the Movement Disorder Society · 2025
    Review
  13. Article
  14. Article
  15. Article
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  19. Article
  20. Pleiotropy of autism-associated chromatin regulators.Development (Cambridge, England) · 2023
    Article

1 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

4 authors at 2 institutions in 1 country.

Yin-Wei KuoDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Olivier TrottierDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Mohammed MahamdehDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Jonathon HowardDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511; jonathon.howard@yale.edu.
Yale University · USHarvard University · US

Funding

Cell Biological Limitations Constrain Dendritic Branching Morphology and Neuronal FunctionDP1MH110065 · NIMH · YALE UNIVERSITY · PI HOWARD, JONATHON · 2015 to 2019
$4.2M
Control of microtubule length by polymerases and depolymerasesR01GM110386 · NIGMS · YALE UNIVERSITY · PI HOWARD, JONATHON · 2014 to 2017
$1.6M
NIGMS NIH HHS R01 GM110386NIMH NIH HHS DP1 MH110065
6 · The paper itself

Abstract

The remodeling of the microtubule cytoskeleton underlies dynamic cellular processes, such as mitosis, ciliogenesis, and neuronal morphogenesis. An important class of microtubule remodelers comprises the severases-spastin, katanin, and fidgetin-which cut microtubules into shorter fragments. While severing activity might be expected to break down the microtubule cytoskeleton, inhibiting these enzymes in vivo actually decreases, rather increases, the number of microtubules, suggesting that severases have a nucleation-like activity. To resolve this paradox, we reconstituted

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsDrosophila melanogasterDrosophila ProteinsMicrotubulesSpastinAdenosine TriphosphatasesAdenosine TriphosphateDrosophila Proteinsspas protein, DrosophilaSpastinmicrotubule dynamicsmicrotubule nucleationseverasesevering enzymespastin

Identifiers

PMID30837315
PMCPMC6431158
OpenAlexW2920404804

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.