Evidence map›Paper›PMID 25390646›Full record

ArticlePloS one2014

Spastin-interacting protein NA14/SSNA1 functions in cytokinesis and axon development.

Uma Goyal, Benoît Renvoisé, Jaerak Chang, Craig Blackstone

Open access · goldAbstract read
In one paragraph

Article in PloS one, 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
0.6field-weighted citation impact, top 40% 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, 32 citations in OpenAlex.

  1. Review
  2. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. ThebioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. The Role of Spastin in Axon Biology.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Cytoskeleton and Membrane Organization at Axon Branches.Frontiers in cell and developmental biology · 2021
    Review
  15. Article
  16. Article
  17. Truncating mutations ofMolecular biology of the cell · 2017
    Article
  18. Article
  19. Review
  20. The Chlamydomonas cell cycle.The Plant journal : for cell and molecular biology · 2015
    Review
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.

Uma GoyalCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.
Benoît RenvoiséCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.
Jaerak ChangCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.
Craig BlackstoneCell Biology Section, Neurogenetics Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, United States of America.
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · US

Funding

Molecular Pathogenesis Of Hereditary Spastic ParaplegiasZIANS002992 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI BLACKSTONE, CRAIG · 2009 to 2021
$20.6M
Howard Hughes Medical InstituteIntramural NIH HHS
6 · The paper itself

Abstract

Hereditary spastic paraplegias (HSPs) are a genetically diverse group of inherited neurological disorders (SPG1-72) with the cardinal feature of prominent lower-extremity spasticity due to a length-dependent axonopathy of corticospinal motor neurons. The most frequent form of autosomal dominant HSP results from mutations of the SPG4 gene product spastin. This is an ATPase associated with diverse cellular activities (AAA) protein that binds to and severs microtubules. While spastin participates in crucial cellular processes such as cytokinesis, endosomal tubulation, and axon development, its role in HSP pathogenesis remains unclear. Spastin interacts in cells with the NA14 protein, a major target for auto-antibodies in Sjögren's syndrome (nuclear autoantigen 1; SSNA1). Our analysis of endogenous spastin and NA14 proteins in HeLa cells and rat cortical neurons in primary culture revealed a clear distribution of both proteins to centrosomes, with NA14 localizing specifically to centrioles. Stable NA14 knockdown in cell lines dramatically affected cell division, in particular cytokinesis. Furthermore, overexpression of NA14 in neurons significantly increased axon outgrowth and branching, while also enhancing neuronal differentiation. We postulate that NA14 may act as an adaptor protein regulating spastin localization to centrosomes, temporally and spatially regulating the microtubule-severing activity of spastin that is particularly critical during the cell cycle and neuronal development.

Indexed as

Adenosine TriphosphatasesAnimalsAutoantigensAxonsCell DifferentiationCentrosomeCerebral CortexCytokinesisGene Expression Regulation, DevelopmentalHeLa CellsHumansMicrotubulesMotor NeuronsNeurogenesisNuclear ProteinsPrimary Cell CultureAdenosine TriphosphatasesAutoantigensNA14 nuclear autoantigenNuclear ProteinsRNA, Small InterferingSpastinSPAST protein, human

Identifiers

PMID25390646
PMCPMC4229207
OpenAlexW2032357399

What OpenQuestion holds

Textmetadata
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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.