Evidence map›Paper›PMID 29065306›Full record

ArticleDevelopmental cell2017

Mitotic Disassembly of Nuclear Pore Complexes Involves CDK1- and PLK1-Mediated Phosphorylation of Key Interconnecting Nucleoporins.

Monika I Linder, Mario Köhler, Paul Boersema, Marion Weberruss, Cornelia Wandke, Joseph Marino, Caroline Ashiono, Paola Picotti, Wolfram Antonin, Ulrike Kutay

Open access · hybridAbstract read
In one paragraph

Article in Developmental cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 140 citations in OpenAlex.

  1. Review
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  4. CabioRxiv : the preprint server for biology · 2026
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  8. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
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26 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 2 countries.

Monika I LinderInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Mario KöhlerInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Paul BoersemaInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Marion WeberrussInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, 52074 Aachen, Germany.
Cornelia WandkeInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Joseph MarinoInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Caroline AshionoInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Paola PicottiInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland.
Wolfram AntoninInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, 52074 Aachen, Germany.
Ulrike KutayInstitute of Biochemistry, Department of Biology, ETH Zurich, 8093 Zurich, Switzerland. Electronic address: ulrike.kutay@bc.biol.ethz.ch.
ETH Zurich · CHRWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During interphase, the nuclear envelope (NE) serves as a selective barrier between cytosol and nucleoplasm. When vertebrate cells enter mitosis, the NE is dismantled in the process of nuclear envelope breakdown (NEBD). Disassembly of nuclear pore complexes (NPCs) is a key aspect of NEBD, required for NE permeabilization and formation of a cytoplasmic mitotic spindle. Here, we show that both CDK1 and polo-like kinase 1 (PLK1) support mitotic NPC disintegration by hyperphosphorylation of Nup98, the gatekeeper nucleoporin, and Nup53, a central nucleoporin linking the inner NPC scaffold to the pore membrane. Multisite phosphorylation of Nup53 critically contributes to its liberation from its partner nucleoporins, including the pore membrane protein NDC1. Initial steps of NPC disassembly in semi-permeabilized cells can be reconstituted by a cocktail of mitotic kinases including cyclinB-CDK1, NIMA, and PLK1, suggesting that the unzipping of nucleoporin interactions by protein phosphorylation is an important principle underlying mitotic NE permeabilization.

Indexed as

CDC2 Protein KinaseCell Cycle ProteinsCell NucleusCyclin-Dependent KinasesHeLa CellsHumansMitosisNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCDC2 Protein KinaseCDK1 protein, humanCell Cycle ProteinsCyclin-Dependent KinasesNuclear Pore Complex ProteinsNup98 protein, humanPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCDK1mitosisNDC1NPCNPC disassemblynucleoporinNup53Nup98phosphorylationPLK1

Identifiers

PMID29065306
PMCPMC5654724
OpenAlexW2766539079

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.