Evidence map›Paper›PMID 11340192›Full record

ArticleThe Plant cell2001

Hyperosmotic stress induces the rapid phosphorylation of a soybean phosphatidylinositol transfer protein homolog through activation of the protein kinases SPK1 and SPK2.

D E Monks, K Aghoram, P D Courtney, D B DeWald, R E Dewey

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
7.7field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 110 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

5 authors at 2 institutions in 1 country.

D E MonksDepartment of Crop Science, North Carolina State University, Raleigh, North Carolina 27695, USA.
K Aghoram
P D Courtney
D B DeWald
R E Dewey
North Carolina State University · USUtah State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although phosphatidylinositol transfer proteins (PITPs) are known to serve critical functions in regulating a varied array of signal transduction processes in animals and yeast, the discovery of a similar class of proteins in plants occurred only recently. Here, we report the participation of Ssh1p, a soybean PITP-like protein, in the early events of osmosensory signal transduction in plants, a function not attributed previously to animal or yeast PITPs. Exposure of plant tissues to hyperosmotic stress led to the rapid phosphorylation of Ssh1p, a modification that decreased its ability to associate with membranes. An osmotic stress-activated Ssh1p kinase activity was detected in several plant species by presenting recombinant Ssh1p as a substrate in in-gel kinase assays. Elements of a similar osmosensory signaling pathway also were conserved in yeast, an observation that facilitated the identification of soybean protein kinases SPK1 and SPK2 as stress-activated Ssh1p kinases. This study reveals the activation of SPK1 and/or SPK2 and the subsequent phosphorylation of Ssh1p as two early successive events in a hyperosmotic stress-induced signaling cascade in plants. Furthermore, Ssh1p is shown to enhance the activities of a plant phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase, an observation that suggests that the ultimate function of Ssh1p in cellular signaling is to alter the plant's capacity to synthesize phosphoinositides during periods of hyperosmotic stress.

Indexed as

Cell Cycle ProteinsMembrane ProteinsCarrier ProteinsCheckpoint Kinase 2Enzyme ActivationGlycine maxModels, BiologicalNicotianaOsmotic PressurePhosphatidylinositol PhosphatesPhosphatidylinositolsPhospholipid Transfer ProteinsPhosphorylationPlant ProteinsPlants, Genetically ModifiedPlants, ToxicCarrier ProteinsCell Cycle ProteinsCheckpoint Kinase 2Membrane Proteinsphosphatidylinositol 3-phosphatephosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsPhospholipid Transfer ProteinsPlant ProteinsProtein Serine-Threonine KinasesRAD53 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID11340192
PMCPMC135558
OpenAlexW2134121217

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.