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Article Dans Une Revue Plant Science Année : 2006

Antagonistic interaction between MAP kinase and protein phosphatase 2C in stress recovery

Résumé

The Arabidopsis mitogen-activated kinase MPK6 transmits a diversity of stress signals. However, much less is known about resetting mechanisms subsequent to the stress response. We show that MPK6 is a potential target of abscisic acid-insensitive 1 (ABI1), a protein phosphatase 2C that acts as a key element in attenuating abscisic acid (ABA)-dependent stress signaling. MPK6 can bind to ABI1 in vitro and in yeast, and that a complex containing these two proteins can be co-precipitated from transfected Arabidopsis cells. In whole plants, MPK6 is hyper-reactive to osmotic stress in mutants compromised in ABI1 activity, but not in its closest functional homolog ABI2. Moreover, conditional expression of a dominant-negative form of mpk6 renders plants hypersensitive to ABA. MPK6 enhances the synthesis of ethylene [1]. ABI1 may therefore down modulate ethylene as part of the resetting mechanism after stress.

Dates et versions

hal-00121497 , version 1 (20-12-2006)

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Jeffrey Leung, Sofia Orfanidi, Françoise Chefdor, Tamás Mészaros, Susanne Bolte, et al.. Antagonistic interaction between MAP kinase and protein phosphatase 2C in stress recovery. Plant Science, 2006, 171 (5), pp.596-606. ⟨10.1016/j.plantsci.2006.06.009⟩. ⟨hal-00121497⟩
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