Evidence map›Paper›PMID 23551663›Full record

ArticleThe Plant journal : for cell and molecular biology2013

The hybrid four-CBS-domain KINβγ subunit functions as the canonical γ subunit of the plant energy sensor SnRK1.

Matthew Ramon, Philip Ruelens, Yi Li, Jen Sheen, Koen Geuten, Filip Rolland

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2013. 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
11.1field-weighted citation impact, top 2% 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, 88 citations in OpenAlex.

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  8. Review
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  10. Heterologous Overexpression of ApplePlants (Basel, Switzerland) · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Genetic Conservation of CBS Domain Containing Protein Family inInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Dynamic Nutrient Signaling Networks in Plants.Annual review of cell and developmental biology · 2021
    Review
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 2 countries.

Matthew RamonKU Leuven Department of Biology, Laboratory of Molecular Plant Biology, Leuven, B-3001, Belgium.
Philip RuelensKU Leuven Department of Biology, Laboratory of Molecular Plant Biology, Leuven, B-3001, Belgium.
Yi LiKU Leuven Department of Biology, Laboratory of Molecular Plant Biology, Leuven, B-3001, Belgium.
Jen SheenDepartment of Molecular Biology and Center for Computational and Integrative Biology, Massachusetts General Hospital, Boston, MA, 02114, USA.
Koen GeutenKU Leuven Department of Biology, Laboratory of Molecular Plant Biology, Leuven, B-3001, Belgium.
Filip RollandKU Leuven Department of Biology, Laboratory of Molecular Plant Biology, Leuven, B-3001, Belgium.
KU Leuven · BEMassachusetts General Hospital · US

Funding

Glucose Signal Transduction Pathways in PlantsR01GM060493 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI SHEEN, JEN · 2000 to 2017
$5.7M
NIGMS NIH HHS R01 GM060493NIGMS NIH HHS R01 GM60493
6 · The paper itself

Abstract

The AMPK/SNF1/SnRK1 protein kinases are a family of ancient and highly conserved eukaryotic energy sensors that function as heterotrimeric complexes. These typically comprise catalytic α subunits and regulatory β and γ subunits, the latter function as the energy-sensing modules of animal AMPK through adenosine nucleotide binding. The ability to monitor accurately and adapt to changing environmental conditions and energy supply is essential for optimal plant growth and survival, but mechanistic insight in the plant SnRK1 function is still limited. In addition to a family of γ-like proteins, plants also encode a hybrid βγ protein that combines the Four-Cystathionine β-synthase (CBS)-domain (FCD) structure in γ subunits with a glycogen-binding domain (GBD), typically found in β subunits. We used integrated functional analyses by ectopic SnRK1 complex reconstitution, yeast mutant complementation, in-depth phylogenetic reconstruction, and a seedling starvation assay to show that only the hybrid KINβγ protein that recruited the GBD around the emergence of the green chloroplast-containing plants, acts as the canonical γ subunit required for heterotrimeric complex formation. Mutagenesis and truncation analysis further show that complex interaction in plant cells and γ subunit function in yeast depend on both a highly conserved FCD and a pre-CBS domain, but not the GBD. In addition to novel insight into canonical AMPK/SNF/SnRK1 γ subunit function, regulation and evolution, we provide a new classification of plant FCD genes as a convenient and reliable tool to predict regulatory partners for the SnRK1 energy sensor and novel FCD gene functions.

Indexed as

Signal TransductionAmino Acid SequenceArabidopsisArabidopsis ProteinsCatalytic DomainCystathionine beta-SynthaseGene Expression Regulation, PlantGenetic Complementation TestModels, MolecularMolecular Sequence DataMultienzyme ComplexesMultigene FamilyMutationPhosphorylationPhylogenyPlant LeavesArabidopsis ProteinsAt3g01090 protein, ArabidopsisCystathionine beta-SynthaseKINbetagamma protein, ArabidopsisMultienzyme ComplexesProtein Serine-Threonine KinasesProtein SubunitsRecombinant Proteins

Identifiers

PMID23551663
PMCPMC6599549
OpenAlexW2158717871

What OpenQuestion holds

Textmetadata
LicenceTDM
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.