Evidence map›Paper›PMID 19590579›Full record

ArticleEMBO reports2009

The SPX domain of the yeast low-affinity phosphate transporter Pho90 regulates transport activity.

Hans Caspar Hürlimann, Benoît Pinson, Martha Stadler-Waibel, Samuel C Zeeman, Florian M Freimoser

Abstract read
In one paragraph

Article in EMBO reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

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  10. Differential Responses ofPlants (Basel, Switzerland) · 2023
    Article
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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.

Hans Caspar HürlimannInstitute of Plant Sciences, ETH Zurich, Universitätstrasse 2, 8092 Zurich, Switzerland.
Benoît Pinson
Martha Stadler-Waibel
Samuel C Zeeman
Florian M Freimoser

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast has two phosphate-uptake systems that complement each other: the high-affinity transporters (Pho84 and Pho89) are active under phosphate starvation, whereas Pho87 and Pho90 are low-affinity transporters that function when phosphate is abundant. Here, we report new regulatory functions of the amino-terminal SPX domain of Pho87 and Pho90. By studying truncated versions of Pho87 and Pho90, we show that the SPX domain limits the phosphate-uptake velocity, suppresses phosphate efflux and affects the regulation of the phosphate signal transduction pathway. Furthermore, split-ubiquitin assays and co-immunoprecipitation suggest that the SPX domain of both Pho90 and Pho87 interacts physically with the regulatory protein Spl2. This work suggests that the SPX domain inhibits low-affinity phosphate transport through a physical interaction with Spl2.

Indexed as

Biological TransportCyclin-Dependent Kinase Inhibitor ProteinsPhosphatesPhosphate Transport ProteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCyclin-Dependent Kinase Inhibitor ProteinsPho90 protein, S cerevisiaePhosphatesPhosphate Transport ProteinsSaccharomyces cerevisiae ProteinsSPL2 protein, S cerevisiae

Identifiers

PMID19590579
PMCPMC2710535

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.