Evidence map›Paper›PMID 17182855›Full record

ArticleMolecular biology of the cell2007

The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo.

Kathryn J Ryan, Yingna Zhou, Susan R Wente

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
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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

3 authors at 1 institution in 1 country.

Kathryn J RyanDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232-8240, USA. kryan@mail.bio.tamu.edu
Yingna Zhou
Susan R Wente
Vanderbilt University Medical Center · US

Funding

REGULATION OF NUCLEAR PORE COMPLEX ASSEMBLYR01GM057438 · NIGMS · WASHINGTON UNIVERSITY · PI HETZER, MARTIN W, WENTE, SUSAN R. · 1998 to 2011
$3.5M
NIGMS NIH HHS R01 GM057438NIGMS NIH HHS R01 GM-57438
6 · The paper itself

Abstract

Nuclear pore complex (NPC) assembly in interphase cells requires that new NPCs insert into an intact nuclear envelope (NE). Our previous work identified the Ran GTPase as an essential component in this process. We proposed that Ran is required for targeting assembly factors to the cytoplasmic NE face via a novel, vesicular intermediate. Although the molecular target was not identified, Ran is known to function by modulating protein interactions for karyopherin (Kap) beta family members. Here we characterize loss-of-function Saccharomyces cerevisiae mutants in KAP95 with blocks in NPC assembly. Similar to defects in Ran cycle mutants, nuclear pore proteins are no longer localized properly to the NE in kap95 mutants. Also like Ran cycle mutants, the kap95-E126K mutant displayed enhanced lethality with nic96 and nup170 mutants. Thus, Kap95 and Ran are likely functioning at the same stage in assembly. However, although Ran cycle mutants accumulate small cytoplasmic vesicles, cells depleted of Kap95 accumulated long stretches of cytoplasmic membranes and had highly distorted NEs. We conclude that Kap95 serves as a key regulator of NPC assembly into intact NEs. Furthermore, both Kap95 and Ran may provide spatial cues necessary for targeting of vesicular intermediates in de novo NPC assembly.

Indexed as

Allelesbeta KaryopherinsCell MembraneCytoplasmGenetic TestingGlutamineLysineModels, BiologicalMutant ProteinsNuclear PoreNuclear Pore Complex ProteinsPhenotypeProtein BindingProtein Transportran GTP-Binding ProteinRecombinant Fusion Proteinsbeta KaryopherinsGlutamineKAP95 protein, S cerevisiaeLysineMutant ProteinsNuclear Pore Complex Proteinsran GTP-Binding ProteinRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17182855
PMCPMC1805111
OpenAlexW2061275835

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.