Evidence map›Paper›PMID 22988299›Full record

ArticleMolecular and cellular biology2012

Reciprocal phosphorylation of yeast glycerol-3-phosphate dehydrogenases in adaptation to distinct types of stress.

Yong Jae Lee, Grace R Jeschke, Françoise M Roelants, Jeremy Thorner, Benjamin E Turk

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

63 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
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3 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 2 countries.

Yong Jae LeeDepartment of Pharmacology, Yale University School of Medicine, New Haven, Connecticut, USA.
Grace R Jeschke
Françoise M Roelants
Jeremy Thorner
Benjamin E Turk
Yale University · USInstitute of Molecular Biology and Biophysics · RU

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
Proteome-wide analysis of kinase phosphorylation specificity in yeastR01GM079498 · NIGMS · YALE UNIVERSITY · PI TURK, BENJAMIN E · 2007 to 2011
$1.8M
YEAST PEPTIDE HORMONE SYNTHESIS AND SIGNAL TRANSDUCTIONR37GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1989 to 1998
–
NIGMS NIH HHS GM021841NIGMS NIH HHS GM102262NIGMS NIH HHS R01 GM021841NIGMS NIH HHS R01 GM079498NIGMS NIH HHS R01 GM102262
6 · The paper itself

Abstract

Eukaryotic cells have evolved mechanisms for ensuring growth and survival in the face of stress caused by a fluctuating environment. Saccharomyces cerevisiae has two homologous glycerol-3-phosphate dehydrogenases, Gpd1 and Gpd2, that are required to endure various stresses, including hyperosmotic shock and hypoxia. These enzymes are only partially redundant, and their unique functions were attributed previously to differential transcriptional regulation and localization. We find that Gpd1 and Gpd2 are negatively regulated through phosphorylation by distinct kinases under reciprocal conditions. Gpd2 is phosphorylated by the AMP-activated protein kinase Snf1 to curtail glycerol production when nutrients are limiting. Gpd1, in contrast, is a target of TORC2-dependent kinases Ypk1 and Ypk2. Inactivation of Ypk1 by hyperosmotic shock results in dephosphorylation and activation of Gpd1, accelerating recovery through increased glycerol production. Gpd1 dephosphorylation acts synergistically with its transcriptional upregulation, enabling long-term growth at high osmolarity. Phosphorylation of Gpd1 and Gpd2 by distinct kinases thereby enables rapid adaptation to specific stress conditions. Introduction of phosphorylation motifs targeted by distinct kinases provides a general mechanism for functional specialization of duplicated genes during evolution.

Indexed as

Gene Expression Regulation, FungalAdaptation, PhysiologicalAmino Acid MotifsBiological EvolutionCell HypoxiaGene DuplicationGlycerolGlycerol-3-Phosphate Dehydrogenase (NAD+)Glycogen Synthase Kinase 3Osmolar ConcentrationOsmotic PressurePhosphorylationProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGlycerolGlycerol-3-Phosphate Dehydrogenase (NAD+)Glycogen Synthase Kinase 3GPD1 protein, S cerevisiaeGPD2 protein, S cerevisiaeMCK1 protein, S cerevisiaeProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesYPK2 protein, S cerevisiae

Identifiers

PMID22988299
PMCPMC3486180
OpenAlexW2122936428

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.