Evidence map›Paper›PMID 26673895›Full record

ArticleeLife2015

A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning.

Koray Kırlı, Samir Karaca, Heinz Jürgen Dehne, Matthias Samwer, Kuan Ting Pan, Christof Lenz, Henning Urlaub, Dirk Görlich

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

148 citing papers in PubMed, 246 citations in OpenAlex.

  1. Trial
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  6. A Deep-Learning Atlas of XPO1-Mediated Nuclear Export at Proteome Scale.bioRxiv : the preprint server for biology · 2026
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88 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

8 authors at 2 institutions in 1 country.

Koray KırlıDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-2289-0652
Samir KaracaDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0003-4211-9053
Heinz Jürgen DehneDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-1068-6697
Matthias SamwerDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0003-4495-8619
Kuan Ting PanBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0001-6974-5324
Christof LenzBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-0946-8166
Henning UrlaubBioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0003-1837-5233
Dirk GörlichDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4343-5210
Max Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CRM1 is a highly conserved, RanGTPase-driven exportin that carries proteins and RNPs from the nucleus to the cytoplasm. We now explored the cargo-spectrum of CRM1 in depth and identified surprisingly large numbers, namely >700 export substrates from the yeast S. cerevisiae, ≈1000 from Xenopus oocytes and >1050 from human cells. In addition, we quantified the partitioning of ≈5000 unique proteins between nucleus and cytoplasm of Xenopus oocytes. The data suggest new CRM1 functions in spatial control of vesicle coat-assembly, centrosomes, autophagy, peroxisome biogenesis, cytoskeleton, ribosome maturation, translation, mRNA degradation, and more generally in precluding a potentially detrimental action of cytoplasmic pathways within the nuclear interior. There are also numerous new instances where CRM1 appears to act in regulatory circuits. Altogether, our dataset allows unprecedented insights into the nucleocytoplasmic organisation of eukaryotic cells, into the contributions of an exceedingly promiscuous exportin and it provides a new basis for NES prediction.

Indexed as

Active Transport, Cell NucleusProteomicsAnimalsExportin 1 ProteinHumansKaryopherinsProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeXenopusExportin 1 ProteinKaryopherinsProteinsReceptors, Cytoplasmic and Nuclearbiochemistrycell biologyexportinhuman<i>s. cerevisiae</i>NESNupprotein localizationprotein transportxenopusXPO1/CRM1

Identifiers

PMID26673895
PMCPMC4764573
OpenAlexW2218364825

What OpenQuestion holds

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LicenceCC BY
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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.