4.7 Article

TaARPC5 is required for wheat defense signaling in response to infection by the stripe rust fungus

Journal

CROP JOURNAL
Volume 10, Issue 1, Pages 88-97

Publisher

KEAI PUBLISHING LTD
DOI: 10.1016/j.cj.2021.01.009

Keywords

ARPC5; Cytoskeleton; Wheat; Puccinia striiformis f. sp. tritici; Virus-induced gene silencing (VIGS)

Funding

  1. National Transgenic Key Project of the Ministry of Agriculture of China [2020ZX08009-15B]
  2. National Natural Science Foundation of China [31972224]
  3. National Key Research and Development Program of China [2018YFD0200402]
  4. Natural Science Basic Research Program of Shaanxi [2020JZ-13]
  5. 111 Project from the Ministry of Education of China [B07049]
  6. Open Project Program of State Key Laboratory of Crop Stress Biology for Arid Areas [CSBAA2020010]

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Numerous studies have shown that the actin cytoskeleton responds dynamically to pathogen infection. In this study, researchers investigated the role of the actin-related protein TaARPC5 in wheat's resistance against Puccinia striiformis f. sp. tritici (Pst) infection. They found that TaARPC5 plays a key role in regulating the host's actin cytoskeleton and resistance signaling, contributing to enhanced resistance against Pst.
Numerous studies using a combination of confocal microscopic- and pharmacological-based approaches have demonstrated that the actin cytoskeleton dynamically responds to pathogen infection. Here, we observed that phalloidin treatment induced actin nucleation, resulting in enhanced resistance of wheat against the stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst). To define the mechanism underpinning this process, we characterized a family of conserved actin-binding proteins, the actin related protein (ARP) family, which controls actin polymerization. Specifically, we identified and characterized a wheat ARPC gene (TaARPC5), which encodes a 136-amino acid protein containing a P16-Arc domain, the smallest subunit of the ARP2/3 complex. TaARPC5 mRNA accumulation was induced following the infection of plants with the avirulent Pst strain, and following the elicitation with flagellin (e.g., flg22) as well. Subcellular localization analysis revealed that TaARPC5 is primarily localized to the cortical actin cytoskeleton, and its precise cellular localizations suggest the proximity to processes correlated with the actin-organelle interface. Upon treatment with virulent Pst, TaARPC5-knockdown plants exhibited a significant reduction in the expression of PTI-specific mRNAs. Conversely, we observed enhanced induction of reactive oxygen species (ROS) accumulation and a decrease in TaCAT1 expression following infection with an incompatible Pst isolate. Together with yeast complementation assays, the current study demonstrates a role for TaARPC5 in resistance signaling in wheat against Pst infection by regulating the host actin cytoskeleton. (C) 2021 Crop Science Society of China and Institute of Crop Science, CAAS. Production and hosting by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.

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