Evidence map›Paper›PMID 15075274›Full record

ArticleEukaryotic cell2004

A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndc1p in nuclear pore assembly.

Corine K Lau, Thomas H Giddings, Mark Winey

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

38 citing papers in PubMed, 56 citations in OpenAlex.

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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.

Corine K LauMCD Biology, University of Colorado-Boulder, Boulder, Colorado 80309-0347, USA.
Thomas H Giddings
Mark Winey
University of Colorado Boulder · US

Funding

MOLECULAR BIOLOGYT32GM007135 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI KRAUTER, KENNETH S · 1985 to 2012
$5.7M
SPINDLE POLES AND NUCLEAR PORES--YEAST NDC1 AND MPS2R01GM059992 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WINEY, MARK · 2000 to 2003
$868k
NIGMS NIH HHS GM-07135NIGMS NIH HHS GM-59992NIGMS NIH HHS R01 GM059992NIGMS NIH HHS T32 GM007135
6 · The paper itself

Abstract

Both the spindle pole body (SPB) and the nuclear pore complex (NPC) are essential organelles embedded in the nuclear envelope throughout the life cycle of the budding yeast Saccharomyces cerevisiae. However, the mechanism by which these two multisubunit structures are inserted into the nuclear envelope during their biogenesis is not well understood. We have previously shown that Ndc1p is the only known integral membrane protein that localizes to both the SPBs and the NPCs and is required for SPB duplication. For this study, we generated a novel temperature-sensitive (ts) allele of NDC1 to investigate the role of Ndc1p at the NPCs. Yeast cells carrying this allele (ndc1-39) failed to insert the SPB into the nuclear envelope at the restrictive temperature. Importantly, the double mutation of ndc1-39 and NPC assembly mutant nic96-1 resulted in cells with enhanced growth defects. While nuclear protein import and NPC distribution in the nuclear envelope were unaffected, ndc1-39 mutants failed to properly incorporate the nucleoporin Nup49p into NPCs. These results provide evidence that Ndc1p is required for NPC assembly in addition to its role in SPB duplication. We postulate that Ndc1p is crucial for the biogenesis of both the SPBs and the NPCs at the step of insertion into the nuclear envelope.

Indexed as

AllelesChromosome SegregationFlow CytometryMembrane ProteinsMicroscopy, FluorescenceMicroscopy, ImmunoelectronNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionSpindle ApparatusTemperatureMembrane ProteinsNDC1 protein, S cerevisiaeNIC96 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNUP49 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID15075274
PMCPMC387647
OpenAlexW2165181977

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.