Evidence map›Paper›PMID 14551257›Full record

ArticleMolecular biology of the cell2003

The role of the polo kinase Cdc5 in controlling Cdc14 localization.

Rosella Visintin, Frank Stegmeier, Angelika Amon

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

53 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
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  5. The signalling lipid PI3,5POpen biology · 2023
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  13. Hog1 activation delays mitotic exit via phosphorylation of Net1.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  14. 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

3 authors at 1 institution in 1 country.

Rosella VisintinCenter for Cancer Research, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Frank Stegmeier
Angelika Amon
Howard Hughes Medical Institute · US

Funding

Regulation of Mitosis by Proteolysis in YeastR01GM056800 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI AMON, ANGELIKA B · 2004 to 2015
$3.4M
REGULATION OF MITOSIS BY PROTEOLYSIS IN YEASTR29GM056800 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI AMON, ANGELIKA B · 1997 to 2003
$738k
NIGMS NIH HHS GM-56800NIGMS NIH HHS R01 GM056800NIGMS NIH HHS R29 GM056800
6 · The paper itself

Abstract

In budding yeast, the protein phosphatase Cdc14 controls exit from mitosis. Its activity is regulated by a competitive inhibitor Cfi1/Net1, which binds to and sequesters Cdc14 in the nucleolus. During anaphase, Cdc14 is released from its inhibitor by the action of two regulatory networks. The Cdc Fourteen Early Anaphase Release (FEAR) network initiates Cdc14 release from Cfi1/Net1 during early anaphase, and the Mitotic Exit Network (MEN) promotes Cdc14 release during late anaphase. Here, we investigate the relationship among FEAR network components and propose an order in which they function to promote Cdc14 release from the nucleolus. Furthermore, we examine the role of the protein kinase Cdc5, which is a component of both the FEAR network and the MEN, in Cdc14 release from the nucleolus. We find that overexpression of CDC5 led to Cdc14 release from the nucleolus in S phase-arrested cells, which correlated with the appearance of phosphorylated forms of Cdc14 and Cfi1/Net1. Cdc5 promotes Cdc14 phosphorylation and, by stimulating the MEN, Cfi1/Net1 phosphorylation. Furthermore, we suggest that Cdc14 release from the nucleolus only occurs when Cdc14 and Cfi1/Net1 are both phosphorylated.

Indexed as

Cell Cycle ProteinsCell NucleolusFungal ProteinsMicroscopy, FluorescenceMitosisModels, MolecularMutationNuclear ProteinsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionCDC14 protein, S cerevisiaeCDC5 protein, S cerevisiaeCell Cycle ProteinsFungal ProteinsNet1 protein, S cerevisiaeNuclear ProteinsProtein KinasesProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsSPO12 protein, S cerevisiae

Identifiers

PMID14551257
PMCPMC266767
OpenAlexW2171302195

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.