Publication Information
Mair et al., 2015
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Abstract
Elife. 2015 Aug 11;4:e05828. doi: 10.7554/eLife.05828.
SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response
in plants.
Mair A(1), Pedrotti L(2), Wurzinger B(1), Anrather D(3), Simeunovic A(1), Weiste
C(2), Valerio C(4), Dietrich K(2), Kirchler T(5), Nägele T(1), Vicente Carbajosa
J(6), Hanson J(7), Baena-González E(4), Chaban C(5), Weckwerth W(1), Dröge-Laser
W(2), Teige M(1).
Author information:
(1)Department of Ecogenomics and Systems Biology, University of Vienna, Vienna,
Austria.
(2)Pharmaceutical Biology, Julius-von-Sachs-Institute, University of Würzburg,
Würzburg, Germany.
(3)Mass Spectrometry Facility, Max F. Perutz Laboratories, University of Vienna,
Vienna, Austria.
(4)Instituto Gulbenkian de Ciência, Oeiras, Portugal.
(5)Department of Plant Physiology, Center for Plant Molecular Biology,
University of Tübingen, Tübingen, Germany.
(6)Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de
Madrid, Madrid, Spain.
(7)Department of Molecular Plant Physiology, Utrecht University, Utrecht,
Netherlands.
Metabolic adjustment to changing environmental conditions, particularly
balancing of growth and defense responses, is crucial for all organisms to
survive. The evolutionary conserved AMPK/Snf1/SnRK1 kinases are well-known
metabolic master regulators in the low-energy response in animals, yeast and
plants. They act at two different levels: by modulating the activity of key
metabolic enzymes, and by massive transcriptional reprogramming. While the first
part is well established, the latter function is only partially understood in
animals and not at all in plants. Here we identified the Arabidopsis
transcription factor bZIP63 as key regulator of the starvation response and
direct target of the SnRK1 kinase. Phosphorylation of bZIP63 by SnRK1 changed
its dimerization preference, thereby affecting target gene expression and
ultimately primary metabolism. A bzip63 knock-out mutant exhibited
starvation-related phenotypes, which could be functionally complemented by wild
type bZIP63, but not by a version harboring point mutations in the identified
SnRK1 target sites.
DOI: 10.7554/eLife.05828
PMCID: PMC4558565
PMID: 26263501 [Indexed for MEDLINE]
Conflict of interest statement: The authors declare that no competing interests
exist.
