Evidence map›Paper›PMID 39092499›Full record

ArticleJournal of cell science2024

N-terminal tags impair the ability of lamin A to provide structural support to the nucleus.

Jacob Odell, Jan Lammerding

Abstract read
In one paragraph

Article in Journal of cell science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
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  9. Article
  10. Biallelic ELOVL1 Variants Are Linked to Hypomyelinating Leukodystrophy, Movement Disorder, and Ichthyosis.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  11. Article
  12. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Jacob OdellWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0001-9043-1338
Jan LammerdingWeill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA.ORCID 0000-0003-4335-8611

Funding

Nuclear mechanics and mechanotransduction in muscular laminopathiesR01HL082792 · NHLBI · CORNELL UNIVERSITY · PI LAMMERDING, JAN · 2007 to 2023
$4.8M
Nuclear mechanobiology in confined migration (Equipment Supplement 2023)R01GM137605 · NIGMS · CORNELL UNIVERSITY · PI LAMMERDING, JAN · 2020 to 2023
$1.6M
Nuclear mechanobiology in confined migration (equipment supplement 2026)R35GM153257 · NIGMS · CORNELL UNIVERSITY · PI Jan Lammerding · 2024 to 2026
$1.3M
National Science Foundation URoL2022048NHLBI NIH HHS R01 HL082792NIGMS NIH HHS R01 GM137605NIGMS NIH HHS R35 GM153257NIH HHS R01 HL082792Volkswagen Foundation A130142
6 · The paper itself

Abstract

Lamins are intermediate filament proteins that contribute to numerous cellular functions, including nuclear morphology and mechanical stability. The N-terminal head domain of lamin is crucial for higher order filament assembly and function, yet the effects of commonly used N-terminal tags on lamin function remain largely unexplored. Here, we systematically studied the effect of two differently sized tags on lamin A (LaA) function in a mammalian cell model engineered to allow for precise control of expression of tagged lamin proteins. Untagged, FLAG-tagged and GFP-tagged LaA completely rescued nuclear shape defects when expressed at similar levels in lamin A/C-deficient (Lmna-/-) MEFs, and all LaA constructs prevented increased nuclear envelope ruptures in these cells. N-terminal tags, however, altered the nuclear localization of LaA and impaired the ability of LaA to restore nuclear deformability and to recruit emerin to the nuclear membrane in Lmna-/- MEFs. Our finding that tags impede some LaA functions but not others might explain the partial loss of function phenotypes when tagged lamins are expressed in model organisms and should caution researchers using tagged lamins to study the nucleus.

Indexed as

Cell NucleusLamin Type ANuclear EnvelopeAnimalsHumansMembrane ProteinsMiceNuclear ProteinsemerinLamin Type AMembrane ProteinsNuclear ProteinsEmerinFluorescent tagsGFPLaminMechanobiologyNucleus

Identifiers

PMID39092499
PMCPMC11361635

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.