Evidence map›Paper›PMID 25644599›Full record

ReviewGenes & development2015

Lamins at the crossroads of mechanosignaling.

Selma Osmanagic-Myers, Thomas Dechat, Roland Foisner

Open access · diamondAbstract readReview
In one paragraph

Review in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
–field-weighted citation impact
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

153 citing papers in PubMed, 225 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Nuclear dysfunction in aging and neurodegeneration.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Downregulation of Nesprin1 by Runx2 deficiency is critical for the development of skeletal laminopathy-like pathology.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

93 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

3 authors at 1 institution in 1 country.

Selma Osmanagic-MyersMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University Vienna, A-1030 Vienna, Austria.
Thomas DechatMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University Vienna, A-1030 Vienna, Austria.
Roland FoisnerMax F. Perutz Laboratories, Department of Medical Biochemistry, Medical University Vienna, A-1030 Vienna, Austria roland.foisner@meduniwien.ac.at.
Max Perutz Labs · AT

Funding

Austrian Science Fund FWF P 26492Austrian Science Fund FWF T 584
6 · The paper itself

Abstract

The intermediate filament proteins, A- and B-type lamins, form the nuclear lamina scaffold adjacent to the inner nuclear membrane. B-type lamins confer elasticity, while A-type lamins lend viscosity and stiffness to nuclei. Lamins also contribute to chromatin regulation and various signaling pathways affecting gene expression. The mechanical roles of lamins and their functions in gene regulation are often viewed as independent activities, but recent findings suggest a highly cross-linked and interdependent regulation of these different functions, particularly in mechanosignaling. In this newly emerging concept, lamins act as a "mechanostat" that senses forces from outside and responds to tension by reinforcing the cytoskeleton and the extracellular matrix. A-type lamins, emerin, and the linker of the nucleoskeleton and cytoskeleton (LINC) complex directly transmit forces from the extracellular matrix into the nucleus. These mechanical forces lead to changes in the molecular structure, modification, and assembly state of A-type lamins. This in turn activates a tension-induced "inside-out signaling" through which the nucleus feeds back to the cytoskeleton and the extracellular matrix to balance outside and inside forces. These functions regulate differentiation and may be impaired in lamin-linked diseases, leading to cellular phenotypes, particularly in mechanical load-bearing tissues.

Indexed as

Mechanotransduction, CellularAnimalsCell MovementExtracellular MatrixGene Expression RegulationHumansLaminsMutationLaminscytoskeletonextracellular matrixlaminsLINC complexmechanosensingmechanotransduction

Identifiers

PMID25644599
PMCPMC4318140
OpenAlexW2127659175

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.