Evidence map›Paper›PMID 20164192›Full record

ArticleThe Journal of biological chemistry2010

Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK) determines their catalytic activities.

Pierre Crozet, Fabien Jammes, Benoit Valot, Françoise Ambard-Bretteville, Sylvie Nessler, Michael Hodges, Jean Vidal, Martine Thomas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

34 citing papers in PubMed, 77 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

8 authors at 3 institutions in 1 country.

Pierre CrozetFrom the Laboratoire de Signalisation et Régulation Métabolique, Institut de Biologie des Plantes, Université Paris-Sud 11, UMR 8618 CNRS, Bâtiment 630, 91405 Orsay Cedex, France.
Fabien Jammes
Benoit Valot
Françoise Ambard-Bretteville
Sylvie Nessler
Michael Hodges
Jean Vidal
Martine Thomas
Université Paris-Sud · FRCentre National de la Recherche Scientifique · FRLaboratoire d'Enzymologie et Biochimie Structurales · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 complexes belong to the SNF1/AMPK/SnRK1 protein kinase family that shares an ancestral function as central regulators of metabolism. In A. thaliana, the products of AtSnAK1 and AtSnAK2, orthologous to yeast genes, have been shown to autophosphorylate and to phosphorylate/activate the AtSnRK1.1 catalytic subunit on Thr(175). The phosphorylation of these kinases has been investigated by site-directed mutagenesis and tandem mass spectrometry. The autophosphorylation site of AtSnAK2 was identified as Thr(154), and it was shown to be required for AtSnAK catalytic activity. Interestingly, activated AtSnRK1 exerted a negative feedback phosphorylation on AtSnAK2 at Ser(261) (Ser(260) of AtSnAK1) that was dependent on AtSnAK autophosphorylation. The dynamics of these reciprocal phosphorylation events on the different kinases was established, and structural modeling allowed clarification of the topography of the AtSnAK phosphorylation sites. A mechanism is proposed to explain the observed changes in the enzymatic properties of each kinase triggered by these phosphorylation events.

Indexed as

Amino Acid SubstitutionArabidopsisArabidopsis ProteinsBinding SitesEnzyme ActivationFeedback, PhysiologicalModels, MolecularMutagenesis, Site-DirectedPhosphorylationProtein ConformationProtein KinasesProtein Serine-Threonine KinasesProtein SubunitsRecombinant ProteinsSucroseTandem Mass SpectrometryArabidopsis ProteinsAt3g01090 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesProtein SubunitsRecombinant ProteinsSucrose

Identifiers

PMID20164192
PMCPMC2852945
OpenAlexW1969571623

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.