Evidence map›Paper›PMID 34970964›Full record

ArticleeLife2021

SSNA1 stabilizes dynamic microtubules and detects microtubule damage.

Elizabeth J Lawrence, Goker Arpag, Cayetana Arnaiz, Marija Zanic

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  4. PMEnvironment & health (Washington, D.C.) · 2026
    Article
  5. 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
  6. Article
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  8. SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026
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  14. ThebioRxiv : the preprint server for biology · 2024
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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.

Elizabeth J LawrenceDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, United States.ORCID 0000-0001-9543-8678
Goker ArpagDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, United States.ORCID 0000-0002-6893-2678
Cayetana ArnaizDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, United States.ORCID 0000-0001-5069-1469
Marija ZanicDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, United States.ORCID 0000-0002-5127-5819
Vanderbilt University · US

Funding

Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Biophysical Principles of Microtubule DynamicsR35GM119552 · NIGMS · VANDERBILT UNIVERSITY · PI Marija Zanic · 2016 to 2026
$4.4M
NCI NIH HHS T32 CA119925NIGMS NIH HHS R35 GM119552
6 · The paper itself

Abstract

Sjögren's syndrome nuclear autoantigen-1 (SSNA1/NA14) is a microtubule-associated protein with important functions in cilia, dividing cells, and developing neurons. However, the direct effects of SSNA1 on microtubules are not known. We employed in vitro reconstitution with purified proteins and TIRF microscopy to investigate the activity of human SSNA1 on dynamic microtubule ends and lattices. Our results show that SSNA1 modulates all parameters of microtubule dynamic instability-slowing down the rates of growth, shrinkage, and catastrophe, and promoting rescue. We find that SSNA1 forms stretches along growing microtubule ends and binds cooperatively to the microtubule lattice. Furthermore, SSNA1 is enriched on microtubule damage sites, occurring both naturally, as well as induced by the microtubule severing enzyme spastin. Finally, SSNA1 binding protects microtubules against spastin's severing activity. Taken together, our results demonstrate that SSNA1 is both a potent microtubule-stabilizing protein and a novel sensor of microtubule damage; activities that likely underlie SSNA1's functions on microtubule structures in cells.

Indexed as

AutoantigensCell LineHumansMicrotubule-Associated ProteinsMicrotubulesNuclear ProteinsSpastinAutoantigensMicrotubule-Associated ProteinsNA14 nuclear autoantigenNuclear ProteinsSpastincell biologycytoskeletonin vitro reconstitutionmicrotubule damagemicrotubule dynamicsmolecular biophysicsnonespastinSSNA1structural biology

Identifiers

PMID34970964
PMCPMC8798045
OpenAlexW4226142736

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.