Evidence map›Paper›PMID 37469276›Full record

ArticleEMBO reports2023

Super-resolution microscopy reveals focal organization of ER-associated Y-complexes in mitosis.

Rojapriyadharshini Gandhimathi, Dorothea Pinotsi, Mario Köhler, Jörg Mansfeld, Caroline Ashiono, Tatjana Kleele, Sumit Pawar, Ulrike Kutay

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
  3. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  4. Review
  5. Article
  6. Article
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.

Rojapriyadharshini GandhimathiDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Dorothea PinotsiScopeM, ETH Zürich, Zürich, Switzerland.
Mario KöhlerDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Jörg MansfeldDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Caroline AshionoDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Tatjana KleeleDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Sumit PawarDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Ulrike KutayDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-8257-7465
ETH Zurich · CHInstitute of Cancer Research · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During mitotic entry of vertebrate cells, nuclear pore complexes (NPCs) are rapidly disintegrated. NPC disassembly is initiated by hyperphosphorylation of linker nucleoporins (Nups), which leads to the dissociation of FG repeat Nups and relaxation of the nuclear permeability barrier. However, less is known about disintegration of the huge nuclear and cytoplasmic rings, which are formed by annular assemblies of Y-complexes that are dissociated from NPCs as intact units. Surprisingly, we observe that Y-complex Nups display slower dissociation kinetics compared with other Nups during in vitro NPC disassembly, indicating a mechanistic difference in the disintegration of Y-based rings. Intriguingly, biochemical experiments reveal that a fraction of Y-complexes remains associated with mitotic ER membranes, supporting recent microscopic observations. Visualization of mitotic Y-complexes by super-resolution microscopy demonstrates that they form two classes of higher order assemblies: large clusters at kinetochores and small, focal ER-associated assemblies. These, however, lack features qualifying them as persisting ring-shaped subassemblies previously proposed to serve as structural templates for NPC reassembly during mitotic exit, which helps to refine current models of nuclear reassembly.

Indexed as

MicroscopyMitosisCell NucleusNuclear PoreNuclear Pore Complex ProteinsNuclear Pore Complex ProteinsmitosisNPC disassemblynuclear pore complexnucleoporinY-complex

Identifiers

PMID37469276
PMCPMC10481662
OpenAlexW4384820348

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.