Evidence map›Paper›PMID 31296869›Full record

ArticleNature communications2019

Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity.

Alex A Makarov, Juan Zou, Douglas R Houston, Christos Spanos, Alexandra S Solovyova, Cristina Cardenal-Peralta, Juri Rappsilber, Eric C Schirmer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

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  12. The NFATc1/P2X7 receptor relationship in human intervertebral disc cells.Frontiers in cell and developmental 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

8 authors at 2 institutions in 2 countries.

Alex A MakarovWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK.ORCID http://orcid.org/0000-0002-0980-1723
Juan ZouWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK.
Douglas R HoustonWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK.
Christos SpanosWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK.ORCID http://orcid.org/0000-0002-4376-8242
Alexandra S SolovyovaInstitute for Cell and Molecular Biosciences/NUPPA, The Medical School, University of Newcastle, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK.
Cristina Cardenal-PeraltaWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK.
Juri RappsilberWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK. juri.rappsilber@ed.ac.uk.ORCID http://orcid.org/0000-0001-5999-1310
Eric C SchirmerWellcome Centre for Cell Biology, University of Edinburgh, Max Born Crescent, Edinburgh, EH9 3BF, UK. e.schirmer@ed.ac.uk.ORCID http://orcid.org/0000-0003-2635-1338
Wellcome Centre for Cell Biology · GBNewcastle University · GB

Funding

Medical Research Council MR/R018073/1Wellcome Trust 103139/Z/13/Z
6 · The paper itself

Abstract

Lamin A is a nuclear intermediate filament protein critical for nuclear architecture and mechanics and mutated in a wide range of human diseases. Yet little is known about the molecular architecture of lamins and mechanisms of their assembly. Here we use SILAC cross-linking mass spectrometry to determine interactions within lamin dimers and between dimers in higher-order polymers. We find evidence for a compression mechanism where coiled coils in the lamin A rod can slide onto each other to contract rod length, likely driven by a wide range of electrostatic interactions with the flexible linkers between coiled coils. Similar interactions occur with unstructured regions flanking the rod domain during oligomeric assembly. Mutations linked to human disease block these interactions, suggesting that this spring-like contraction can explain in part the dynamic mechanical stretch and flexibility properties of the lamin polymer and other intermediate filament networks.

Indexed as

Amino Acid SequenceAnimalsCardiomyopathy, DilatedCross-Linking ReagentsElasticityHumansIntermediate Filament ProteinsLamin Type AMass SpectrometryMuscular DystrophiesMutationNuclear EnvelopeNuclear MatrixProtein DomainsProtein MultimerizationProtein Structure, SecondaryCross-Linking ReagentsIntermediate Filament ProteinsLamin Type ALMNA protein, humanRecombinant Proteins

Identifiers

PMID31296869
PMCPMC6624373
OpenAlexW2960691556

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.