Evidence map›Paper›PMID 18178775›Full record

ArticleEukaryotic cell2008

Requirement for the budding yeast polo kinase Cdc5 in proper microtubule growth and dynamics.

Chong J Park, Jung-Eun Park, Tatiana S Karpova, Nak-Kyun Soung, Li-Rong Yu, Sukgil Song, Kyung H Lee, Xue Xia, Eugene Kang, Ilknur Dabanoglu and 8 more

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.6field-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

30 citing papers in PubMed, 41 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

18 authors at 4 institutions in 2 countries.

Chong J ParkLaboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Jung-Eun Park
Tatiana S Karpova
Nak-Kyun Soung
Li-Rong Yu
Sukgil Song
Kyung H Lee
Xue Xia
Eugene Kang
Ilknur Dabanoglu
Doo-Yi Oh
James Y Zhang
Young Hwi Kang
Stephen Wincovitch
Tim C Huffaker
Timothy D Veenstra
James G McNally
Kyung S Lee
Cornell University · USGene Therapy Laboratory · FRNational Institutes of Health · USNational Cancer Institute · US

Funding

NHGRI/DIR Cytogenetics and Microscopy CoreZICHG200348 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI WINCOVITCH, STEPHEN · 2010 to 2025
$20.3M
MOLECULAR ANALYSIS OF MICROTUBULE FUNCTION IN YEASTR01GM040479 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HUFFAKER, TIM C · 1988 to 2010
$2.6M
Fluorescence Imaging FacilityZICBC010571 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MCNALLY, JAMES G · 2009 to 2013
$1.3M
Intramural NIH HHSNCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NIGMS NIH HHS R01 GM040479
6 · The paper itself

Abstract

In many organisms, polo kinases appear to play multiple roles during M-phase progression. To provide new insights into the function of the budding yeast polo kinase Cdc5, we generated novel temperature-sensitive cdc5 mutants by mutagenizing the C-terminal noncatalytic polo box domain, a region that is critical for proper subcellular localization. One of these mutants, cdc5-11, exhibited a temperature-sensitive growth defect with an abnormal spindle morphology. Strikingly, provision of a moderate level of benomyl, a microtubule-depolymerizing drug, permitted cdc5-11 cells to grow significantly better than the isogenic CDC5 wild type in a FEAR (cdc Fourteen Early Anaphase Release)-independent manner. In addition, cdc5-11 required MAD2 for both cell growth and the benomyl-remedial phenotype. These results suggest that cdc5-11 is defective in proper spindle function. Consistent with this view, cdc5-11 exhibited abnormal spindle morphology, shorter spindle length, and delayed microtubule regrowth at the nonpermissive temperature. Overexpression of CDC5 moderately rescued the spc98-2 growth defect. Interestingly, both Cdc28 and Cdc5 were required for the proper modification of the spindle pole body components Nud1, Slk19, and Stu2 in vivo. They also phosphorylated these three proteins in vitro. Taken together, these observations suggest that concerted action of Cdc28 and Cdc5 on Nud1, Slk19, and Stu2 is important for proper spindle functions.

Indexed as

Spindle ApparatusCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsDeoxyribonucleasesMicrotubule-Associated ProteinsMicrotubulesProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinstRNA MethyltransferasesCDC28 Protein Kinase, S cerevisiaeCDC5 protein, S cerevisiaeCell Cycle ProteinsDeoxyribonucleasesMicrotubule-Associated ProteinsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSlk19 protein, S cerevisiaeSTU2 protein, S cerevisiaeTRM2 protein, S cerevisiaetRNA Methyltransferases

Identifiers

PMID18178775
PMCPMC2268509
OpenAlexW2158933095

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.