Evidence map›Paper›PMID 15470255›Full record

ArticleEukaryotic cell2004

PP2A phosphatase activity is required for stress and Tor kinase regulation of yeast stress response factor Msn2p.

Arti Santhanam, Alan Hartley, Katrin Düvel, James R Broach, Stephen Garrett

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 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed, 104 citations in OpenAlex.

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  11. Transcription FactorJournal of fungi (Basel, Switzerland) · 2021
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  12. HJournal of fungi (Basel, Switzerland) · 2021
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4 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Arti SanthanamDepartment of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, Newark, NJ 07101, USA.
Alan Hartley
Katrin Düvel
James R Broach
Stephen Garrett
Princeton University · USRutgers, The State University of New Jersey · US

Funding

VIRAL AND CELLULAR ONCOGENES--MECHANISM OF ACTIONP01CA041086 · NCI · PRINCETON UNIVERSITY · PI WIESCHAUS, ERIC F · 1986 to 2005
$9.4M
GENETIC ANALYSIS OF GROWTH AND CELL CYCLE IN YEASTR01GM044666 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI GARRETT, STEPHEN · 1991 to 2003
$1.2M
NCI NIH HHS CA41086NCI NIH HHS P01 CA041086NIGMS NIH HHS GM44666NIGMS NIH HHS R01 GM044666
6 · The paper itself

Abstract

In response to stress and nutrient starvation, the Saccharomyces cerevisiae transcription factor Msn2p accumulates in the nucleus and activates expression of a broad array of genes. Here, we analyze the role of the Tor (target of rapamycin) signaling pathway in mediating these responses. Inactivation of the Tor pathway component Tap42p using tap42(Ts) alleles causes a sustained nuclear localization similar to that after the addition of the Tor kinase inhibitor rapamycin. Effects of Tap42p inactivation and rapamycin addition could be suppressed by deletion of TIP41, which encodes a Tap42p-interacting protein. These results support the notion that rapamycin affects Msn2p by inactivating Tap42p function. Tap42p interacts with the catalytic subunit of PP2A (protein phosphatase 2A) and PP2A-like phosphatases. Deletion of either the catalytic or regulatory subunit that forms the PP2A phosphatase complex prevents nuclear accumulation of Msn2p in the tap42(Ts) strain and in wild-type strains treated with rapamycin. These results suggest that Tap42p is an inhibitor of PP2A phosphatase, which in turn inhibits nuclear export of Msn2p. Interestingly, PP2A function is also required for nuclear accumulation of Msn2p in response to stresses, such as heat and osmotic shock, as well as nitrogen (but not glucose) starvation. Thus, PP2A and the Tor kinase pathway transduce stress and nitrogen starvation signals to Msn2p. Finally, Msn2p localization is unaffected by conditional loss of 14-3-3 protein function, ruling out the possibility that 14-3-3 proteins act as a scaffold to sequester Msn2p in the cytoplasm.

Indexed as

14-3-3 ProteinsAdaptor Proteins, Signal TransducingCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsGenes, FungalNitrogenPhosphatidylinositol 3-KinasesPhosphoprotein PhosphatasesPhosphotransferases (Alcohol Group Acceptor)Protein Phosphatase 2Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSirolimusTranscription Factors14-3-3 ProteinsAdaptor Proteins, Signal TransducingBMH1 protein, S cerevisiaeBMH2 protein, S cerevisiaeCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsMSN2 protein, S cerevisiaeNitrogenPhosphatidylinositol 3-KinasesPhosphoprotein PhosphatasesPhosphotransferases (Alcohol Group Acceptor)Protein Phosphatase 2Saccharomyces cerevisiae ProteinsSirolimusTAP42 protein, S cerevisiaeTOR1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID15470255
PMCPMC522594
OpenAlexW2137653823

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.