Evidence map›Paper›PMID 29514856›Full record

ArticleJournal of cell science2018

Mitotic spindle assembly and γ-tubulin localisation depend on the integral nuclear membrane protein Samp1.

Veronica J Larsson, Mohammed Hakim Jafferali, Balaje Vijayaraghavan, Ricardo A Figueroa, Einar Hallberg

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Observational
  6. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
  7. Nuclear envelope remodelling during mitosis.Current opinion in cell biology · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. The Biology of the Nuclear Envelope and Its Implications in Cancer Biology.International journal of molecular sciences · 2019
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. 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

5 authors at 1 institution in 1 country.

Veronica J LarssonDepartment of Neurochemistry, Stockholm University, SE-106 91 Stockholm, Sweden.
Mohammed Hakim JafferaliDepartment of Neurochemistry, Stockholm University, SE-106 91 Stockholm, Sweden.
Balaje VijayaraghavanDepartment of Neurochemistry, Stockholm University, SE-106 91 Stockholm, Sweden.
Ricardo A FigueroaDepartment of Neurochemistry, Stockholm University, SE-106 91 Stockholm, Sweden.
Einar HallbergDepartment of Neurochemistry, Stockholm University, SE-106 91 Stockholm, Sweden einar.hallberg@neurochem.su.se.ORCID 0000-0003-2092-457X
Stockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have investigated a possible role for the inner nuclear membrane protein Samp1 (also known as TMEM201) in the mitotic machinery. Live-cell imaging showed that Samp1a-YFP (Samp1a is the short isoform of Samp1) distributed as filamentous structures in the mitotic spindle, partially colocalising with β-tubulin. Samp1 depletion resulted in an increased frequency of cells with signs of chromosomal mis-segregation and prolonged metaphase, indicating problems with spindle assembly and/or chromosomal alignment. Consistent with this, mitotic spindles in Samp1-depleted cells contained significantly lower levels of β-tubulin and γ-tubulin, phenotypes that were rescued by overexpression of Samp1a-YFP. We found that Samp1 can bind directly to γ-tubulin and that Samp1 co-precipitated with γ-tubulin and the HAUS6 subunit of the Augmin complex in live cells. The levels of HAUS6, in the mitotic spindle also decreased after Samp1 depletion. We show that Samp1 is involved in the recruitment of HAUS6 and γ-tubulin to the mitotic spindle. Samp1 is the first inner nuclear membrane protein shown to have a function in mitotic spindle assembly.

Indexed as

HumansMembrane ProteinsNuclear ProteinsSpindle ApparatusTubulinMembrane ProteinsNuclear ProteinsTMEM201 protein, humanTubulinAugminCancerMitotic spindleNuclear membraneSamp1γ-Tubulin

Identifiers

PMID29514856
PMCPMC5963844
OpenAlexW2792806394

What OpenQuestion holds

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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.