Evidence map›Paper›PMID 11729145›Full record

ArticleGenetics2001

The Spo12 protein of Saccharomyces cerevisiae: a regulator of mitotic exit whose cell cycle-dependent degradation is mediated by the anaphase-promoting complex.

R Shah, S Jensen, L M Frenz, A L Johnson, L H Johnston

Abstract read
In one paragraph

Article in Genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

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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

5 authors.

R ShahNational Institute for Medical Research, Medical Research Council, London NW7 1AA, United Kingdom.
S Jensen
L M Frenz
A L Johnson
L H Johnston

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Spo12 protein plays a regulatory role in two of the most fundamental processes of biology, mitosis and meiosis, and yet its biochemical function remains elusive. In this study we concentrate on the genetic and biochemical analysis of its mitotic function. Since high-copy SPO12 is able to suppress a wide variety of mitotic exit mutants, all of which arrest with high Clb-Cdc28 activity, we speculated whether SPO12 is able to facilitate exit from mitosis when overexpressed by antagonizing mitotic kinase activity. We show, however, that Spo12 is not a potent regulator of Clb-Cdc28 activity and can function independently of either the cyclin-dependent kinase inhibitor (CDKi), Sic1, or the anaphase-promoting complex (APC) regulator, Hct1. Spo12 protein level is regulated by the APC and the protein is degraded in G1 by an Hct1-dependent mechanism. We also demonstrate that in addition to localizing to the nucleus Spo12 is a nucleolar protein. We propose a model where overexpression of Spo12 may lead to the delocalization of a small amount of Cdc14 from the nucleolus, resulting in a sufficient lowering of mitotic kinase levels to facilitate mitotic exit. Finally, site-directed mutagenesis of highly conserved residues in the Spo12 protein sequence abolishes both its mitotic suppressor activity as well as its meiotic function. This result is the first indication that Spo12 may carry out the same biochemical function in mitosis as it does in meiosis.

Indexed as

MitosisProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnaphaseCDC28 Protein Kinase, S cerevisiaeCdh1 ProteinsCell CycleCell Cycle ProteinsCell NucleolusCell NucleusCyclin BCyclin-Dependent Kinase Inhibitor ProteinsCyclin-Dependent KinasesDiploidyFluorescent Antibody Technique, IndirectCDC14 protein, S cerevisiaeCDC28 Protein Kinase, S cerevisiaeCdh1 ProteinsCDH1 protein, S cerevisiaeCell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BCyclin-Dependent Kinase Inhibitor ProteinsCyclin-Dependent KinasesDBF20 protein, S cerevisiaeDBF2 protein, S cerevisiaeFungal ProteinsGalactoseGlucoseNuclear ProteinsProtein KinasesProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesSaccharomyces cerevisiae ProteinsSIC1 protein, S cerevisiaeSPO12 protein, S cerevisiae

Identifiers

PMID11729145
PMCPMC1461877

What OpenQuestion holds

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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.