4.8 Article

Oxylipin signaling in salt-stressed soybean is modulated by ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase

Journal

PLANT CELL
Volume 34, Issue 3, Pages 1117-1143

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/plcell/koab306

Keywords

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Funding

  1. Hong Kong Research Grants Council Area of Excellence Scheme [AoE/M-403/16]
  2. Innovation and Technology Fund
  3. Wilson and Amelia Wong Endowment Fund

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Phosphatidic acid signaling and alternative splicing play a crucial role in inhibiting the ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase, triggering oxylipin signaling in salt-stressed soybean. The discovery highlights a dual mechanism that initiates the onset of oxylipin signaling in response to salinity.
Phosphatidic acid signaling and alternative splicing inhibit ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase, triggering oxylipin signaling in salt-stressed soybean. Plant lipoxygenases (LOXs) oxygenate linoleic and linolenic acids, creating hydroperoxy derivatives, and from these, jasmonates and other oxylipins are derived. Despite the importance of oxylipin signaling, its activation mechanism remains largely unknown. Here, we show that soybean ACYL-COA-BINDING PROTEIN3 (ACBP3) and ACBP4, two Class II acyl-CoA-binding proteins, suppressed activity of the vegetative LOX homolog VLXB by sequestering it at the endoplasmic reticulum. The ACBP4-VLXB interaction was facilitated by linoleoyl-CoA and linolenoyl-CoA, which competed with phosphatidic acid (PA) for ACBP4 binding. In salt-stressed roots, alternative splicing produced ACBP variants incapable of VLXB interaction. Overexpression of the variants enhanced LOX activity and salt tolerance in Arabidopsis and soybean hairy roots, whereas overexpressors of the native forms exhibited reciprocal phenotypes. Consistently, the differential alternative splicing pattern in two soybean genotypes coincided with their difference in salt-induced lipid peroxidation. Salt-treated soybean roots were enriched in C32:0-PA species that showed high affinity to Class II ACBPs. We conclude that PA signaling and alternative splicing suppress ligand-dependent interaction of Class II ACBPs with VLXB, thereby triggering lipid peroxidation during salt stress. Hence, our findings unveil a dual mechanism that initiates the onset of oxylipin signaling in the salinity response.

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