Evidence map›Paper›PMID 25895666›Full record

ArticleeLife2015

A non-canonical mechanism for Crm1-export cargo complex assembly.

Ute Fischer, Nico Schäuble, Sabina Schütz, Martin Altvater, Yiming Chang, Marius Boulos Faza, Vikram Govind Panse

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

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  11. Eukaryotic Ribosome assembly and Nucleocytoplasmic Transport.Methods in molecular biology (Clifton, N.J.) · 2022
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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

7 authors at 1 institution in 1 country.

Ute FischerInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Nico SchäubleInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Sabina SchützInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Martin AltvaterInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Yiming ChangInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Marius Boulos FazaInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Vikram Govind PanseInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transport receptor Crm1 mediates the export of diverse cargos containing leucine-rich nuclear export signals (NESs) through complex formation with RanGTP. To ensure efficient cargo release in the cytoplasm, NESs have evolved to display low affinity for Crm1. However, mechanisms that overcome low affinity to assemble Crm1-export complexes in the nucleus remain poorly understood. In this study, we reveal a new type of RanGTP-binding protein, Slx9, which facilitates Crm1 recruitment to the 40S pre-ribosome-associated NES-containing adaptor Rio2. In vitro, Slx9 binds Rio2 and RanGTP, forming a complex. This complex directly loads Crm1, unveiling a non-canonical stepwise mechanism to assemble a Crm1-export complex. A mutation in Slx9 that impairs Crm1-export complex assembly inhibits 40S pre-ribosome export. Thus, Slx9 functions as a scaffold to optimally present RanGTP and the NES to Crm1, therefore, triggering 40S pre-ribosome export. This mechanism could represent one solution to the paradox of weak binding events underlying rapid Crm1-mediated export.

Indexed as

Active Transport, Cell NucleusCell NucleusEpistasis, GeneticExportin 1 ProteinKaryopherinsMultiprotein ComplexesMutationNuclear Export SignalsProtein BindingProtein Transportran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRibosomesSaccharomyces cerevisiaeExportin 1 ProteinKaryopherinsMultiprotein ComplexesNuclear Export Signalsran GTP-Binding ProteinReceptors, Cytoplasmic and Nuclearbiochemistrycell biologyCrm1/Xpo1nuclear export signalsnuclear transportribosome exportRio2S. cerevisiaeSlx9

Identifiers

PMID25895666
PMCPMC4402694
OpenAlexW2153431837

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.