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Phosphatidylethanolamines link ferroptosis and autophagy during appressorium formation of rice blast fungus

Qiao Liu1, Ruhui Long1, Chaoxiang Lin1

  • 1State Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, Guangdong Province Key Laboratory of Microbial Signals and Disease Control, Integrative Microbiology Research Centre, South China Agricultural University, Guangzhou, China.

Molecular Plant Pathology
|July 3, 2024
PubMed

Insights

Ferroptosis, a cell death pathway, is crucial for the rice blast fungus Magnaporthe oryzae's pathogenicity. This study identifies lysophosphatidic acid acyltransferase (Lpaat) as essential for ferroptosis and links lipid metabolism to autophagy.

Area of Science:

  • Mycology
  • Cell Biology
  • Biochemistry

Background:

  • Ferroptosis, a regulated cell death pathway, is vital for the rice blast fungus Magnaporthe oryzae's infection structure development.
  • Lysophosphatidic acid acyltransferase (Lpaat) function and its role in fungal ferroptosis and pathogenicity remain largely uncharacterized.

Purpose of the Study:

  • To investigate the role of Lpaat in fungal ferroptosis, pathogenicity, and its connection to lipid metabolism and autophagy in Magnaporthe oryzae.
  • To elucidate the specific phosphatidylethanolamine (PE) species regulated by Lpaat and their impact on cellular processes.

Main Methods:

  • Gene identification and knockout of the orthologous Lpaat gene in Magnaporthe oryzae.
  • Analysis of ferroptosis induction via lipid peroxidation.
  • Assessment of autophagy pathway activation using the autophagy protein Atg8.
  • Subcellular localization studies of GFP-tagged Lpaat using lipid droplet staining.

Main Results:

  • Lpaat is essential for fungal ferroptosis and pathogenicity in Magnaporthe oryzae.
  • Specific PE species (DOPE and SLPE), dependent on Lpaat, induce lipid peroxidation and ferroptosis.
  • DOPE and SLPE positively regulate autophagy, and Lpaat deficiency impairs Atg8 lipidation, indicating an autophagy defect.
  • Lpaat localizes to lipid droplet membranes, suggesting their role as a lipid source for PE biosynthesis and autophagosome formation.

Conclusions:

  • Lpaat plays a critical role in linking lipid metabolism, ferroptosis, and autophagy in Magnaporthe oryzae.
  • Lipid droplets are implicated as a source for membrane PE biosynthesis and potentially autophagosome biogenesis.
  • This study reveals novel intracellular membrane-bound organelle dynamics mediated by Lpaat.
Keywords:
Magnaporthe oryzaecell deathferroptosislysophosphatidic acid acetyltransferase (Lpaat)phosphatidylethanolamine (PE)

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