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<p>Rice blast caused by <i>Magnaporthe oryzae</i> poses a major threat to world food supply. Conditions conducive to the disease include insufficient light. Our previous studies found that light-dependent phosphorylation of light-harvesting complex II protein (LHCB5) mediates rice immunity; however, the underlying mechanisms, in particular, the upstream regulators of LHCB5 phosphorylation, remain unknown. Here, we show that OsLIKE1 functions as a lectin receptor-like kinase (LecRLK) to play a critical role in rice resistance against <i>M. oryzae</i>. OsLIKE1 interacts with and phosphorylates LHCB5. In addition, we find two phosphorylation sites in the kinase domain of OsLIKE1 important for its auto-phosphorylation and phosphorylation of LHCB5. Moreover, we find that variation in light-induced OsLIKE1 expression is driven by specific single-nucleotide polymorphisms (SNPs) within the promoter region. These SNPs promote the auto-phosphorylation of OsLIKE1 to phosphorylate LHCB5 and activate its immune function against the blast fungus. Collectively, these findings elucidate the mechanism by which light regulates OsLIKE1-dependent defense in rice and support SNP-based rice breeding programs that increase disease resistance.</p>

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Light-induced OsLIKE1 phosphorylation enhances rice resistance against blast disease

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月23日

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  • Jiangtao Liu,
  • Lei Su,
  • Wenya Wang,
  • Jintao Wang,
  • Weizhong Chen,
  • Zhixiang Yang,
  • Leiyun Yang,
  • Gang Li,
  • Xinyu Liu,
  • Haifeng Zhang,
  • Zhongqiang Qi,
  • Yongfeng Liu,
  • Yuqiang Liu,
  • Ping Wang,
  • Muxing Liu,
  • Zhengguang Zhang

摘要

Rice blast caused by Magnaporthe oryzae poses a major threat to world food supply. Conditions conducive to the disease include insufficient light. Our previous studies found that light-dependent phosphorylation of light-harvesting complex II protein (LHCB5) mediates rice immunity; however, the underlying mechanisms, in particular, the upstream regulators of LHCB5 phosphorylation, remain unknown. Here, we show that OsLIKE1 functions as a lectin receptor-like kinase (LecRLK) to play a critical role in rice resistance against M. oryzae. OsLIKE1 interacts with and phosphorylates LHCB5. In addition, we find two phosphorylation sites in the kinase domain of OsLIKE1 important for its auto-phosphorylation and phosphorylation of LHCB5. Moreover, we find that variation in light-induced OsLIKE1 expression is driven by specific single-nucleotide polymorphisms (SNPs) within the promoter region. These SNPs promote the auto-phosphorylation of OsLIKE1 to phosphorylate LHCB5 and activate its immune function against the blast fungus. Collectively, these findings elucidate the mechanism by which light regulates OsLIKE1-dependent defense in rice and support SNP-based rice breeding programs that increase disease resistance.