Evidence map›Paper›PMID 32537912›Full record

ArticleEMBO reports2020

Nuclear envelope rupture and NET formation is driven by PKCα-mediated lamin B disassembly.

Yubin Li, Minghui Li, Bettina Weigel, Moritz Mall, Victoria P Werth, Ming-Lin Liu

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 98 citations in OpenAlex.

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  16. Protein Kinase C Regulates Meiosis in Mammalian Oocytes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  17. Characterizing Keratinocyte-Derived Extracellular Vesicles in UVB-Irradiated Murine Skin.JID innovations : skin science from molecules to population health · 2026
    Article
  18. Article
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9 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

6 authors at 3 institutions in 3 countries.

Yubin LiCorporal Michael J. Crescenz VAMC, Philadelphia, PA, USA.
Minghui LiCorporal Michael J. Crescenz VAMC, Philadelphia, PA, USA.
Bettina WeigelCell Fate Engineering and Disease Modeling Group, German Cancer Research Center (DKFZ) and DKFZ-ZMBH Alliance, Heidelberg, Germany.
Moritz MallCell Fate Engineering and Disease Modeling Group, German Cancer Research Center (DKFZ) and DKFZ-ZMBH Alliance, Heidelberg, Germany.
Victoria P WerthCorporal Michael J. Crescenz VAMC, Philadelphia, PA, USA.
Ming-Lin LiuCorporal Michael J. Crescenz VAMC, Philadelphia, PA, USA.ORCID 0000-0001-8827-2024
Philadelphia VA Medical Center · USGerman Cancer Research Center · DETianjin Medical University General Hospital · CN

Funding

Extracellular vesicle-associated MAVS and IFNẞ in DermatomyositisR21AI144838 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI LIU, MING-LIN · 2019 to 2020
$443k
BLRD VA I01 BX000706| H2020 Priority Excellent Science | H2020 European Research Council (ERC) 804710Lupus Research Alliance (LRA) 416805NIAID NIH HHS R21 AI144838U.S. Department of Veterans Affairs (VA) 5I01BX000706
6 · The paper itself

Abstract

The nuclear lamina is essential for the structural integration of the nuclear envelope. Nuclear envelope rupture and chromatin externalization is a hallmark of the formation of neutrophil extracellular traps (NETs). NET release was described as a cellular lysis process; however, this notion has been questioned recently. Here, we report that during NET formation, nuclear lamin B is not fragmented by destructive proteolysis, but rather disassembled into intact full-length molecules. Furthermore, we demonstrate that nuclear translocation of PKCα, which serves as the kinase to induce lamin B phosphorylation and disassembly, results in nuclear envelope rupture. Decreasing lamin B phosphorylation by PKCα inhibition, genetic deletion, or by mutating the PKCα consensus sites on lamin B attenuates extracellular trap formation. In addition, strengthening the nuclear envelope by lamin B overexpression attenuates NET release in vivo and reduces levels of NET-associated inflammatory cytokines in UVB-irradiated skin of lamin B transgenic mice. Our findings advance the mechanistic understanding of NET formation by showing that PKCα-mediated lamin B phosphorylation drives nuclear envelope rupture for chromatin release in neutrophils.

Indexed as

Lamin Type BNuclear EnvelopeAnimalsLamin Type AMiceNuclear LaminaPhosphorylationProtein Kinase C-alphaLamin Type ALamin Type BProtein Kinase C-alphalamin B disassemblyNET formationnuclear envelope rupturePKCα

Identifiers

PMID32537912
PMCPMC7403722
OpenAlexW3035432909

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.