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MPK12 in stomatal CO2 signaling: function beyond its kinase activity.

Chung-Yueh Yeh1, Yuh-Shuh Wang1, Yohei Takahashi2

  • 1Institute of Technology, University of Tartu, Nooruse 1, Tartu, 50411, Estonia.

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Summary

Mitogen-activated protein kinase 12 (MPK12) regulates stomatal closure by binding to HT1 kinase, independent of its own kinase activity. This interaction acts as a molecular switch for guard cells sensing atmospheric carbon dioxide (CO2) levels.

Keywords:
CO2 signalingHT1MAP kinase 12allosteric inhibitionguard cellnoncatalytic activitystomata

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Area of Science:

  • Plant physiology
  • Molecular signaling
  • Biochemistry

Background:

  • Protein phosphorylation regulates stomatal opening and closure.
  • The interaction between MAP kinase 12 (MPK12) and Raf-like kinase HT1 is crucial for CO2-induced stomatal movements.

Purpose of the Study:

  • To investigate the role of MPK12 kinase activity in CO2-induced stomatal responses.
  • To examine the noncatalytic function of MPK12 in guard cell CO2 signaling via allosteric inhibition of HT1.

Main Methods:

  • Genetic analysis of plant lines with modified MPK12 versions.
  • Biochemical assays to study protein interactions.
  • Structural modeling to elucidate the MPK12:HT1 interface.

Main Results:

  • CO2/HCO3- enhanced MPK12-HT1 interaction is independent of MPK12 kinase activity.
  • CO2-dependent stomatal responses require MPK12 binding to HT1, not its kinase function.
  • Purified MPK12 and HT1 form a heterodimer in the presence of CO2/HCO3-.

Conclusions:

  • MPK12 acts as a molecular switch in guard cells for sensing atmospheric CO2.
  • The kinase-activity-independent interaction between MPK12 and HT1 is key to this sensing mechanism.