Evidence map›Paper›PMID 33771882›Full record

ArticleMolecular cancer research : MCR2021

Defects in Emerin-Nucleoskeleton Binding Disrupt Nuclear Structure and Promote Breast Cancer Cell Motility and Metastasis.

Alexandra G Liddane, Chelsea A McNamara, Mallory C Campbell, Isabelle Mercier, James M Holaska

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cancer research : MCR, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  8. Article
  9. The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  10. Article
  11. Review
  12. Review
  13. Emerin expression stratification across breast cancer subtypes.Cancer treatment and research communications · 2025
    Article
  14. Article
  15. Article
  16. Emerin deficiency drives MCF7 cells to an invasive phenotype.bioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Alexandra G LiddaneDepartment of Pharmaceutical Sciences, University of the Sciences, Philadelphia, Pennsylvania.
Chelsea A McNamaraDepartment of Biomedical Sciences, Cooper Medical School of Rowan University, Camden, New Jersey.ORCID 0000-0002-2178-8453
Mallory C CampbellDepartment of Pharmaceutical Sciences, University of the Sciences, Philadelphia, Pennsylvania.
Isabelle MercierDepartment of Pharmaceutical Sciences, University of the Sciences, Philadelphia, Pennsylvania.
James M HolaskaDepartment of Pharmaceutical Sciences, University of the Sciences, Philadelphia, Pennsylvania. holaska@rowan.edu.
University of the Sciences · USCooper Medical School of Rowan University · US

Funding

Emerin regulation of myogenic differentiation: implications for muscle diseaseR15AR069935 · NIAMS · UNIVERSITY OF THE SCIENCES PHILADELPHIA · PI JAMES Michael HOLASKA · 2016 to 2026
$2.0M
NIAMS NIH HHS R15 AR069935
6 · The paper itself

Abstract

Nuclear envelope proteins play an important role in regulating nuclear size and structure in cancer. Altered expression of nuclear lamins are found in many cancers and its expression is correlated with better clinical outcomes. The nucleus is the largest organelle in the cell with a diameter between 10 and 20 μm. Nuclear size significantly impacts cell migration. Nuclear structural changes are predicted to impact cancer metastasis by regulating cancer cell migration. Here we show emerin regulates nuclear structure in invasive breast cancer cells to impact cancer metastasis. Invasive breast cancer cells had 40% to 50% less emerin than control cells, which resulted in decreased nuclear size. Overexpression of GFP-emerin in invasive breast cancer cells rescued nuclear size and inhibited migration through 3.0 and 8.0 μm pores. Mutational analysis showed emerin binding to nucleoskeletal proteins was important for its regulation of nuclear structure, migration, and invasion. Importantly, emerin expression inhibited lung metastasis by 91% in orthotopic mouse models of breast cancer. Emerin nucleoskeleton-binding mutants failed to inhibit metastasis. These results support a model whereby emerin binding to the nucleoskeleton regulates nuclear structure to impact metastasis. In this model, emerin plays a central role in metastatic transformation, because decreased emerin expression during transformation causes the nuclear structural defects required for increased cell migration, intravasation, and extravasation. IMPLICATIONS: Modulating emerin expression and function represents new targets for therapeutic interventions of metastasis, because increased emerin expression rescued cancer metastasis.

Indexed as

AnimalsBreast NeoplasmsCell CycleCell LineCell Line, TumorCell MovementCell NucleusCell ProliferationCells, CulturedFemaleGreen Fluorescent ProteinsHumansMembrane ProteinsMiceMice, NudeMicroscopy, ConfocalemerinGreen Fluorescent ProteinsMembrane ProteinsNuclear Proteins

Identifiers

PMID33771882
PMCPMC8254762
OpenAlexW3136752470

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.