Evidence map›Paper›PMID 33570570›Full record

ArticleThe Journal of cell biology2021

Computational analyses reveal spatial relationships between nuclear pore complexes and specific lamins.

Mark Kittisopikul, Takeshi Shimi, Meltem Tatli, Joseph Riley Tran, Yixian Zheng, Ohad Medalia, Khuloud Jaqaman, Stephen A Adam, Robert D Goldman

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
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  6. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
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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

9 authors at 4 institutions in 3 countries.

Mark Kittisopikul *Department of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.
Takeshi Shimi *Department of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.
Meltem TatliDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Joseph Riley TranDepartment of Embryology, Carnegie Institution for Science, Baltimore, MD.
Yixian ZhengDepartment of Embryology, Carnegie Institution for Science, Baltimore, MD.
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Khuloud JaqamanDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX.
Stephen A AdamDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.
Robert D GoldmanDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.
Northwestern University · USJanelia Research Campus · USCarnegie Institution for Science · USUniversity of Zurich · CH

Funding

Mechanisms and Functional Consequences of Signaling Protein Organization at MembranesR35GM119619 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI DASGUPTA, APARAJITA KAMALESH · 2016 to 2025
$4.3M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
Super-resolution microscopy of nuclear lamin and spindle envelope/matrix functionR01GM106023 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI GOLDMAN, ROBERT D, ZHENG, YIXIAN · 2013 to 2020
$3.5M
Nikon Super-Resolution Structured Illumination Microscope (SIM)S10OD016342 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CHEW, TENG-LEONG · 2013 to 2013
$600k
NCI NIH HHS T32 CA080621NIGMS NIH HHS R01 GM106023NIGMS NIH HHS R35 GM119619NIH HHS S10 OD016342
6 · The paper itself

Abstract

Nuclear lamin isoforms form fibrous meshworks associated with nuclear pore complexes (NPCs). Using datasets prepared from subpixel and segmentation analyses of 3D-structured illumination microscopy images of WT and lamin isoform knockout mouse embryo fibroblasts, we determined with high precision the spatial association of NPCs with specific lamin isoform fibers. These relationships are retained in the enlarged lamin meshworks of Lmna-/- and Lmnb1-/- fibroblast nuclei. Cryo-ET observations reveal that the lamin filaments composing the fibers contact the nucleoplasmic ring of NPCs. Knockdown of the ring-associated nucleoporin ELYS induces NPC clusters that exclude lamin A/C fibers but include LB1 and LB2 fibers. Knockdown of the nucleoporin TPR or NUP153 alters the arrangement of lamin fibers and NPCs. Evidence that the number of NPCs is regulated by specific lamin isoforms is presented. Overall the results demonstrate that lamin isoforms and nucleoporins act together to maintain the normal organization of lamin meshworks and NPCs within the nuclear envelope.

Indexed as

Computer SimulationAnimalsCell LineEmbryo, MammalianFibroblastsLamin Type ALamin Type BMiceMice, KnockoutNuclear PoreNuclear Pore Complex ProteinsLamin Type ALamin Type BLmna protein, mouseNuclear Pore Complex ProteinsNup153 protein, mouse

Identifiers

PMID33570570
PMCPMC7883741
OpenAlexW3126428450

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.