Evidence map›Paper›PMID 25831502›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Systematic identification of signal integration by protein kinase A.

Marie Filteau, Guillaume Diss, Francisco Torres-Quiroz, Alexandre K Dubé, Andrea Schraffl, Verena A Bachmann, Isabelle Gagnon-Arsenault, Andrée-Ève Chrétien, Anne-Lise Steunou, Ugo Dionne and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Advances inJournal of fungi (Basel, Switzerland) · 2023
    Review
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  10. Autophagy and the endolysosomal system in presynaptic function.Cellular and molecular life sciences : CMLS · 2021
    Review
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  20. Distributed and dynamic intracellular organization of extracellular information.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

14 authors at 3 institutions in 2 countries.

Marie FilteauDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.
Guillaume DissDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.
Francisco Torres-QuirozDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.ORCID http://orcid.org/0000-0002-3073-8546
Alexandre K DubéDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.
Andrea SchrafflInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck, University of Innsbruck, A-6020 Innsbruck, Austria; and.
Verena A BachmannInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck, University of Innsbruck, A-6020 Innsbruck, Austria; and.
Isabelle Gagnon-ArsenaultDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.
Andrée-Ève ChrétienDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes.
Anne-Lise SteunouDépartement de Biologie Moléculaire, Biochimie Médicale et Pathologie, and Centre de Recherche sur le Cancer, Université Laval, Québec, QC, G1V 0A6, Canada; Centre de Recherche du Centre Hospitalier Universitaire de Québec, Québec, QC, G1R 2J6, Canada.
Ugo DionneDépartement de Biologie Moléculaire, Biochimie Médicale et Pathologie, and Centre de Recherche sur le Cancer, Université Laval, Québec, QC, G1V 0A6, Canada; Centre de Recherche du Centre Hospitalier Universitaire de Québec, Québec, QC, G1R 2J6, Canada.
Jacques CôtéDépartement de Biologie Moléculaire, Biochimie Médicale et Pathologie, and Centre de Recherche sur le Cancer, Université Laval, Québec, QC, G1V 0A6, Canada; Centre de Recherche du Centre Hospitalier Universitaire de Québec, Québec, QC, G1R 2J6, Canada.ORCID http://orcid.org/0000-0001-6751-555X
Nicolas BissonThe Quebec Network for Research on Protein Function, Structure, and Engineering, Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, and Centre de Recherche sur le Cancer, Université Laval, Québec, QC, G1V 0A6, Canada; Centre de Recherche du Centre Hospitalier Universitaire de Québec, Québec, QC, G1R 2J6, Canada.
Eduard StefanInstitute of Biochemistry and Center for Molecular Biosciences Innsbruck, University of Innsbruck, A-6020 Innsbruck, Austria; and.
Christian R LandryDépartement de Biologie, The Quebec Network for Research on Protein Function, Structure, and Engineering, Institut de Biologie Intégrative et des Systèmes, Christian.landry@bio.ulaval.ca.
PROTEO · CACentre hospitalier universitaire de Québec · CAUniversität Innsbruck · AT

Funding

Austrian Science Fund FWF P 22608CIHR 299432CIHR 324265CIHR MOP-14308
6 · The paper itself

Abstract

Cellular processes and homeostasis control in eukaryotic cells is achieved by the action of regulatory proteins such as protein kinase A (PKA). Although the outbound signals from PKA directed to processes such as metabolism, growth, and aging have been well charted, what regulates this conserved regulator remains to be systematically identified to understand how it coordinates biological processes. Using a yeast PKA reporter assay, we identified genes that influence PKA activity by measuring protein-protein interactions between the regulatory and the two catalytic subunits of the PKA complex in 3,726 yeast genetic-deletion backgrounds grown on two carbon sources. Overall, nearly 500 genes were found to be connected directly or indirectly to PKA regulation, including 80 core regulators, denoting a wide diversity of signals regulating PKA, within and beyond the described upstream linear pathways. PKA regulators span multiple processes, including the antagonistic autophagy and methionine biosynthesis pathways. Our results converge toward mechanisms of PKA posttranslational regulation by lysine acetylation, which is conserved between yeast and humans and that, we show, regulates protein complex formation in mammals and carbohydrate storage and aging in yeast. Taken together, these results show that the extent of PKA input matches with its output, because this kinase receives information from upstream and downstream processes, and highlight how biological processes are interconnected and coordinated by PKA.

Indexed as

Signal TransductionAcetylationAmino Acid SequenceAnimalsAutophagyCyclic AMPCyclic AMP-Dependent Protein KinasesGalactoseGlucoseHEK293 CellsHomeostasisHumansLuciferases, RenillaMethionineMolecular Sequence DataPhylogenyCyclic AMPCyclic AMP-Dependent Protein KinasesGalactoseGlucoseLuciferases, RenillaMethionineSaccharomyces cerevisiae ProteinsTOR Serine-Threonine KinasesacetylationautophagymethionineRas/cAMP/PKA pathwayTOR

Identifiers

PMID25831502
PMCPMC4394313
OpenAlexW2119921227

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.