Evidence map›Paper›PMID 38605278›Full record

ArticleEMBO reports2024

Phosphorylation of ELYS promotes its interaction with VAPB at decondensing chromosomes during mitosis.

Christina James, Ulrike Möller, Christiane Spillner, Sabine König, Olexandr Dybkov, Henning Urlaub, Christof Lenz, Ralph H Kehlenbach

Open access · diamondAbstract read
In one paragraph

Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  4. Article
  5. Review
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 3 institutions in 1 country.

Christina JamesDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg-August-University Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.ORCID 0000-0002-7443-929X
Ulrike MöllerDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg-August-University Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Christiane SpillnerDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg-August-University Göttingen, Humboldtallee 23, 37073, Göttingen, Germany.
Sabine KönigBioanalytics Group, Institute of Clinical Chemistry, University Medical Center Göttingen, Robert-Koch-Straße 40, 37075, Göttingen, Germany.
Olexandr DybkovBioanalytical Mass Spectrometry Group, Max-Planck-Institute for Multidisciplinary Sciences, Am Fassberg 11, 37077, Göttingen, Germany.ORCID 0000-0001-6005-7242
Henning UrlaubBioanalytics Group, Institute of Clinical Chemistry, University Medical Center Göttingen, Robert-Koch-Straße 40, 37075, Göttingen, Germany.
Christof LenzBioanalytics Group, Institute of Clinical Chemistry, University Medical Center Göttingen, Robert-Koch-Straße 40, 37075, Göttingen, Germany.ORCID 0000-0002-0946-8166
Ralph H KehlenbachDepartment of Molecular Biology, Faculty of Medicine, GZMB, Georg-August-University Göttingen, Humboldtallee 23, 37073, Göttingen, Germany. rkehlen@gwdg.de.ORCID 0000-0003-4920-9916
University of Göttingen · DEUniversitätsmedizin Göttingen · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

Deutsche Forschungsgemeinschaft (DFG) SFB1190,P07Deutsche Forschungsgemeinschaft (DFG) SFB1190,Z02
6 · The paper itself

Abstract

ELYS is a nucleoporin that localizes to the nuclear side of the nuclear pore complex (NPC) in interphase cells. In mitosis, it serves as an assembly platform that interacts with chromatin and then with nucleoporin subcomplexes to initiate post-mitotic NPC assembly. Here we identify ELYS as a major binding partner of the membrane protein VAPB during mitosis. In mitosis, ELYS becomes phosphorylated at many sites, including a predicted FFAT (two phenylalanines in an acidic tract) motif, which mediates interaction with the MSP (major sperm protein)-domain of VAPB. Binding assays using recombinant proteins or cell lysates and co-immunoprecipitation experiments show that VAPB binds the FFAT motif of ELYS in a phosphorylation-dependent manner. In anaphase, the two proteins co-localize to the non-core region of the newly forming nuclear envelope. Depletion of VAPB results in prolonged mitosis, slow progression from meta- to anaphase and in chromosome segregation defects. Together, our results suggest a role of VAPB in mitosis upon recruitment to or release from ELYS at the non-core region of the chromatin in a phosphorylation-dependent manner.

Indexed as

DNA-Binding ProteinsMitosisProtein BindingTranscription FactorsVesicular Transport ProteinsAnaphaseChromatinChromosome SegregationHeLa CellsHumansMembrane ProteinsNuclear EnvelopeNuclear Pore Complex ProteinsPhosphorylationAHCTF1 protein, humanChromatinDNA-Binding ProteinsMembrane ProteinsNuclear Pore Complex ProteinsTranscription FactorsVAPB protein, humanVesicular Transport ProteinsELYSFFAT-motifMitosisNuclear EnvelopeVAPB

Identifiers

PMID38605278
PMCPMC11094025
OpenAlexW4394726940

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.