SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants

Mair, Andrea and Pedrotti, Lorenzo and Wurzinger, Bernhard and Anrather, Dorothea and Simeunovic, Andrea and Weiste, Christoph and Valerio, Concetta and Dietrich, Katrin and Kirchler, Tobias and Naegele, Thomas and Vicente Carbajosa, Jesus and Hanson, Johannes and Baena González, Elena and Chaban, Christina and Weckwerth, Wolfram and Dröege-Laser, Wolfgang and Teige, Markus (2015). SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants. "eLIFE", v. 4 ; pp. 1-33. ISSN 2050-084X. https://doi.org/10.7554/eLife.05828.

Description

Title: SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants
Author/s:
  • Mair, Andrea
  • Pedrotti, Lorenzo
  • Wurzinger, Bernhard
  • Anrather, Dorothea
  • Simeunovic, Andrea
  • Weiste, Christoph
  • Valerio, Concetta
  • Dietrich, Katrin
  • Kirchler, Tobias
  • Naegele, Thomas
  • Vicente Carbajosa, Jesus
  • Hanson, Johannes
  • Baena González, Elena
  • Chaban, Christina
  • Weckwerth, Wolfram
  • Dröege-Laser, Wolfgang
  • Teige, Markus
Item Type: Article
Título de Revista/Publicación: eLIFE
Date: 2015
ISSN: 2050-084X
Volume: 4
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

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.

Funding Projects

TypeCodeAcronymLeaderTitle
FP7264474MERITUniversiteit Utrecht / University of UtrechtMetabolic Reprogramming by Induction of Transcription

More information

Item ID: 41452
DC Identifier: http://oa.upm.es/41452/
OAI Identifier: oai:oa.upm.es:41452
DOI: 10.7554/eLife.05828
Official URL: https://elifesciences.org/content/4/e05828
Deposited by: Memoria Investigacion
Deposited on: 01 Jul 2016 17:54
Last Modified: 01 Jul 2016 17:54
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