Phosphatidic acid mediates salt stress response by regulation of MPK6 in Arabidopsis thaliana

Authors


Author for correspondence:
Wenhua Zhang
Tel: +86 25 84399022
Email: whzhang@njau.edu.cn

Summary

  • Phospholipase D (PLD) hydrolyzes phospholipids to produce phosphatidic acid (PA) and a head group, and is involved in the response to various environmental stresses, including salinity. Here, we determined the roles of PLDα and PA in the mediation of salt (NaCl)-stress signaling through the regulation of mitogen-activated protein kinase (MAPK or MPK) in Arabidopsis thaliana.
  • NaCl-induced changes in the content and composition of PA were quantitatively profiled by electrospray ionization–tandem mass spectrometry (ESI-MS/MS). A specific PA species (a MAPK 16:0–18:2 PA), which was increased in abundance by exposure to NaCl, bound to a MPK6, according to filter binding and ELISA. The effect of PA on MPK6 activity was tested using in-gel analysis.
  • 16:0–18:2 PA stimulated the activity of MPK6 immunoprecipitated from Arabidopsis leaf extracts. Treatment with NaCl induced a transient activation of MPK6 in wild-type plant, but the activation was abolished in the pldα1 plant mutant. A plasma membrane Na+/H+ antiporter (SOS1) was identified as a downstream target of MPK6. MPK6 phosphorylated the C-terminal fragment of SOS1. The MPK6 phosphorylation of SOS1 was stimulated by treatment with NaCl, as well as directly by PA.
  • These results suggest that PA plays a critical role in coupling MAPK cascades in response to salt stress.

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