Evidence map›Paper›PMID 9151683›Full record

ArticleThe Journal of cell biology1997

A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p.

M K Iovine, S R Wente

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

36 citing papers in PubMed, 84 citations in OpenAlex.

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  12. Transport into and out of the nucleus.Microbiology and molecular biology reviews : MMBR · 2001
    Review
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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

2 authors at 1 institution in 1 country.

M K IovineDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
S R Wente
Washington University in St. Louis · US

Funding

TRAINING PROGRAM IN CELLULAR AND MOLECULAR BIOLOGYT32GM007067 · NIGMS · WASHINGTON UNIVERSITY · PI TRUE-KROB, HEATHER L · 1985 to 2020
$20.4M
Molecular Analysis of Nuclear Pore Complex FunctionR37GM051219 · NIGMS · VANDERBILT UNIVERSITY · PI WENTE, SUSAN R. · 2010 to 2019
$5.6M
MOLECULAR ANALYSIS OF NUCLEAR PORE COMPLEX FUNCTIONR01GM051219 · NIGMS · WASHINGTON UNIVERSITY · PI WENTE, SUSAN R. · 1994 to 2009
$4.2M
NIGMS NIH HHS 2T32GM07067-21NIGMS NIH HHS GM51219-02NIGMS NIH HHS R01 GM051219NIGMS NIH HHS R37 GM051219NIGMS NIH HHS T32 GM007067
6 · The paper itself

Abstract

During nuclear import, cytosolic transport factors move through the nuclear pore complex (NPC) to the nuclear compartment. Kap95p is required during import for docking the nuclear localization signal-receptor and ligand to the NPC. Recycling of this factor back to the cytoplasm is necessary for continued rounds of import; however, the mechanism for Kap95p recycling is unknown. We have determined that recycling of Kap95p requires a nuclear export signal (NES). A region containing the NES in Kap95p was sufficient to mediate active nuclear export in a microinjection assay. Moreover, the NES was necessary for function. Mutation of the NES in Kap95p resulted in a temperaturesensitive import mutant, and immunofluorescence microscopy experiments showed that the mutated Kap95p was not recycled but instead localized in the nucleus and at the nuclear envelope. Srp1p, the yeast nuclear localization signal-receptor, also accumulated in the nuclei of the arrested kap95 mutant cells. Wild-type and NES-mutated Kap95p both bound Gsp1p (the yeast Ran/TC4 homologue), Srp1p, and the FXFG repeat region of the nucleoporin Nup1p. In contrast, the NES mutation abolished Kap95p interaction with the GLFG repeat regions from the nucleoporins Nup116p and Nup100p. In vivo interaction was demonstrated by isolation of Kap95p from yeast nuclear lysates in either protein A-tagged Nup116p or protein A-tagged Nup100p complexes. The protein A-tagged Nup116p complex also specifically contained Gle2p. These results support a model in which a step in the recycling of Kap95p is mediated by interaction of an NES with GLFG regions. Analysis of genetic interactions suggests Nup116p has a primary role in Kap95p recycling, with Nup100p compensating in the absence of Nup116p. This finding highlights an important role for a subfamily of GLFG nucleoporins in nuclear export processes.

Indexed as

Nuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid Sequencebeta KaryopherinsBiological TransportCell NucleusFungal ProteinsMembrane ProteinsMicroscopy, ConfocalNuclear ProteinsProtein BindingSaccharomyces cerevisiaeStructure-Activity Relationshipbeta KaryopherinsFungal ProteinsMembrane ProteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP100 protein, S cerevisiaeNUP116 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID9151683
PMCPMC2139834
OpenAlexW2142371650

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Registered trials

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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.