Evidence map›Paper›PMID 27160050›Full record

ArticleNature communications2016

The RanBP2/RanGAP1*SUMO1/Ubc9 SUMO E3 ligase is a disassembly machine for Crm1-dependent nuclear export complexes.

Tobias Ritterhoff, Hrishikesh Das, Götz Hofhaus, Rasmus R Schröder, Annette Flotho, Frauke Melchior

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
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  5. Article
  6. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Modulation of the cytoskeleton for cancer therapy.Frontiers in cell and developmental biology · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    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

6 authors at 3 institutions in 2 countries.

Tobias RitterhoffZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Hrishikesh DasZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Götz HofhausCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, Heidelberg 69120, Germany.
Rasmus R SchröderCryo Electron Microscopy, CellNetworks, BioQuant, Universitätsklinikum Heidelberg, Heidelberg 69120, Germany.
Annette FlothoZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Frauke MelchiorZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
DKFZ-ZMBH Alliance · DEHeidelberg University · DEUniversity Hospital Heidelberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Continuous cycles of nucleocytoplasmic transport require disassembly of transport receptor/Ran-GTP complexes in the cytoplasm. A basic disassembly mechanism in all eukaryotes depends on soluble RanGAP and RanBP1. In vertebrates, a significant fraction of RanGAP1 stably interacts with the nucleoporin RanBP2 at a binding site that is flanked by FG-repeats and Ran-binding domains, and overlaps with RanBP2's SUMO E3 ligase region. Here, we show that the RanBP2/RanGAP1*SUMO1/Ubc9 complex functions as an autonomous disassembly machine with a preference for the export receptor Crm1. We describe three in vitro reconstituted disassembly intermediates, which show binding of a Crm1 export complex via two FG-repeat patches, cargo-release by RanBP2's Ran-binding domains and retention of free Crm1 at RanBP2 after Ran-GTP hydrolysis. Intriguingly, all intermediates are compatible with SUMO E3 ligase activity, suggesting that the RanBP2/RanGAP1*SUMO1/Ubc9 complex may link Crm1- and SUMO-dependent functions.

Indexed as

Active Transport, Cell NucleusExportin 1 ProteinGTPase-Activating ProteinsHEK293 CellsHeLa CellsHumansIn Vitro TechniquesKaryopherinsModels, MolecularMolecular ChaperonesMultiprotein ComplexesNuclear PoreNuclear Pore Complex ProteinsProtein Interaction Domains and MotifsReceptors, Cytoplasmic and NuclearRecombinant ProteinsExportin 1 ProteinGTPase-Activating ProteinsKaryopherinsMolecular ChaperonesMultiprotein ComplexesNuclear Pore Complex Proteinsran-binding protein 2RANGAP1 protein, humanReceptors, Cytoplasmic and NuclearRecombinant ProteinsSUMO-1 ProteinSUMO1 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligases

Identifiers

PMID27160050
PMCPMC4866044
OpenAlexW2366926581

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.