Evidence map›Paper›PMID 28640691›Full record

ArticleNucleus (Austin, Tex.)2017

The nesprin-cytoskeleton interface probed directly on single nuclei is a mechanically rich system.

Daniel A Balikov, Sonia K Brady, Ung Hyun Ko, Jennifer H Shin, Jose M de Pereda, Arnoud Sonnenberg, Hak-Joon Sung, Matthew J Lang

Open access · goldAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

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  8. BiallelicGenes · 2021
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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

8 authors at 6 institutions in 5 countries.

Daniel A Balikova Department of Biomedical Engineering , Vanderbilt University , Nashville , TN , USA.
Sonia K Bradyb Department of Chemical and Biomolecular Engineering , Vanderbilt University , Nashville , TN , USA.
Ung Hyun Koc Department of Mechanical Engineering , Korea Advanced Institute of Science and Technology , Daejeon , Korea.
Jennifer H Shinc Department of Mechanical Engineering , Korea Advanced Institute of Science and Technology , Daejeon , Korea.
Jose M de Peredad Instituto de Biologia Molecular y Celular del Cancer, Consejo Superior de Investigaciones Cientificas , University of Salamanca , Salamanca , Spain.ORCID 0000-0002-8912-6739
Arnoud Sonnenberge Netherlands Cancer Institute , Amsterdam , The Netherlands.ORCID 0000-0001-9585-468X
Hak-Joon Sunga Department of Biomedical Engineering , Vanderbilt University , Nashville , TN , USA.
Matthew J Langb Department of Chemical and Biomolecular Engineering , Vanderbilt University , Nashville , TN , USA.
Korea Advanced Institute of Science and Technology · KRVanderbilt University · USConsejo Superior de Investigaciones Científicas · ESNational University of Singapore · SGThe Netherlands Cancer Institute · NLYonsei University · KR

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007347 · NIGMS · VANDERBILT UNIVERSITY · PI WILLIAMS, CHRISTOPHER S. · 1985 to 2023
$26.3M
NIGMS NIH HHS T32 GM007347
6 · The paper itself

Abstract

The cytoskeleton provides structure and plays an important role in cellular function such as migration, resisting compression forces, and transport. The cytoskeleton also reacts to physical cues such as fluid shear stress or extracellular matrix remodeling by reorganizing filament associations, most commonly focal adhesions and cell-cell cadherin junctions. These mechanical stimuli can result in genome-level changes, and the physical connection of the cytoskeleton to the nucleus provides an optimal conduit for signal transduction by interfacing with nuclear envelope proteins, called nesprins, within the LINC (linker of the nucleus to the cytoskeleton) complex. Using single-molecule on single nuclei assays, we report that the interactions between the nucleus and the cytoskeleton, thought to be nesprin-cytoskeleton interactions, are highly sensitive to force magnitude and direction depending on whether cells are historically interfaced with the matrix or with cell aggregates. Application of ∼10-30 pN forces to these nesprin linkages yielded structural transitions, with a base transition size of 5-6 nm, which are speculated to be associated with partial unfoldings of the spectrin domains of the nesprins and/or structural changes of histones within the nucleus.

Indexed as

Mechanical PhenomenaSingle-Cell AnalysisBiomechanical PhenomenaCell NucleusCytoskeletonHumansMesenchymal Stem CellsNuclear ProteinsNuclear Proteinsbiomechanicscytoskeletonnesprinnucleussingle molecule

Identifiers

PMID28640691
PMCPMC5703230
OpenAlexW2653056493

What OpenQuestion holds

Textmetadata
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.