Evidence map›Paper›PMID 11251069›Full record

ArticleMolecular biology of the cell2001

The nuclear export receptor Xpo1p forms distinct complexes with NES transport substrates and the yeast Ran binding protein 1 (Yrb1p).

P Maurer, M Redd, J Solsbacher, F R Bischoff, M Greiner, A V Podtelejnikov, M Mann, K Stade, K Weis, G Schlenstedt

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

31 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. 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

10 authors at 4 institutions in 3 countries.

P MaurerMedizinische Biochemie und Molekularbiologie, Universität des Saarlandes, 66421 Homburg, Germany.
M Redd
J Solsbacher
F R Bischoff
M Greiner
A V Podtelejnikov
M Mann
K Stade
K Weis
G Schlenstedt
Saarland University · DEUniversity of California, Berkeley · USUniversity of Southern Denmark · DKGerman Cancer Research Center · DE

Funding

Structure and function of the nuclear pore complexR01GM058065 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI HEALD, REBECCA W · 1998 to 2015
$4.6M
NIGMS NIH HHS GM 58065NIGMS NIH HHS R01 GM058065
6 · The paper itself

Abstract

Xpo1p (Crm1p) is the nuclear export receptor for proteins containing a leucine-rich nuclear export signal (NES). Xpo1p, the NES-containing protein, and GTP-bound Ran form a complex in the nucleus that translocates across the nuclear pore. We have identified Yrb1p as the major Xpo1p-binding protein in Saccharomyces cerevisiae extracts in the presence of GTP-bound Gsp1p (yeast Ran). Yrb1p is cytoplasmic at steady-state but shuttles continuously between the cytoplasm and the nucleus. Nuclear import of Yrb1p is mediated by two separate nuclear targeting signals. Export from the nucleus requires Xpo1p, but Yrb1p does not contain a leucine-rich NES. Instead, the interaction of Yrb1p with Xpo1p is mediated by Gsp1p-GTP. This novel type of export complex requires the acidic C-terminus of Gsp1p, which is dispensable for the binding to importin beta-like transport receptors. A similar complex with Xpo1p and Gsp1p-GTP can be formed by Yrb2p, a relative of Yrb1p predominantly located in the nucleus. Yrb1p also functions as a disassembly factor for NES/Xpo1p/Gsp1p-GTP complexes by displacing the NES protein from Xpo1p/Gsp1p. This Yrb1p/Xpo1p/Gsp1p complex is then completely dissociated after GTP hydrolysis catalyzed by the cytoplasmic GTPase activating protein Rna1p.

Indexed as

KaryopherinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsActive Transport, Cell NucleusAmino Acid SequenceCarrier ProteinsExportin 1 ProteinFungal ProteinsGuanosine TriphosphateMacromolecular SubstancesMolecular Sequence DataMonomeric GTP-Binding ProteinsNuclear Localization SignalsNuclear ProteinsSaccharomyces cerevisiaeCarrier ProteinsExportin 1 ProteinFungal ProteinsGSP1 protein, S cerevisiaeGuanosine TriphosphateKaryopherinsMacromolecular SubstancesMonomeric GTP-Binding ProteinsNuclear Localization SignalsNuclear ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID11251069
PMCPMC30962
OpenAlexW2135232555

What OpenQuestion holds

Textmetadata
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.