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<p>Grain size is an important agronomic trait and influences both grain yield and quality in crops. The atypical heterotrimeric Gγ protein subunit GS3 is a central regulator of grain length in rice, and the loss-of-function allele of its corresponding gene has been widely utilized by breeders to improve grain length in rice. Here we report that the CC-type glutaredoxin WG1/OsGRX8 has disulfide oxidoreductase activity and regulates redox state of GS3, thereby determining grain length in rice. GS3 can form dimers and oligomers by intermolecular disulfide bonds, and the cysteine-rich C-terminal region of GS3 is predominantly required for its oligomerization. The oligomerization of GS3 alleviates its inhibitory effect on the interaction between RGB1 and DEP1/GGC2, resulting in an increase in grain length. WG1 interacts with GS3 and reduces the oligomerization of GS3 through redox mechanisms, which causes a decrease in grain length. Genetic analyses support WG1 and GS3 function in a common pathway to control grain length. Thus, our findings reveal a previously unrecognized mechanism, in which redox regulation of a Gγ subunit by a glutaredoxin controls grain length, opening a novel perspective for G protein signaling regulation.</p>

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Redox regulation of G protein oligomerization and signaling by the glutaredoxin WG1 controls grain size in rice

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年5月19日

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  • Lijie Liu,
  • Jianqin Hao,
  • Ke Huang,
  • Penggen Duan,
  • Baolan Zhang,
  • Zhihai Chi,
  • Xiaohong Yao,
  • Yunhai Li

摘要

Grain size is an important agronomic trait and influences both grain yield and quality in crops. The atypical heterotrimeric Gγ protein subunit GS3 is a central regulator of grain length in rice, and the loss-of-function allele of its corresponding gene has been widely utilized by breeders to improve grain length in rice. Here we report that the CC-type glutaredoxin WG1/OsGRX8 has disulfide oxidoreductase activity and regulates redox state of GS3, thereby determining grain length in rice. GS3 can form dimers and oligomers by intermolecular disulfide bonds, and the cysteine-rich C-terminal region of GS3 is predominantly required for its oligomerization. The oligomerization of GS3 alleviates its inhibitory effect on the interaction between RGB1 and DEP1/GGC2, resulting in an increase in grain length. WG1 interacts with GS3 and reduces the oligomerization of GS3 through redox mechanisms, which causes a decrease in grain length. Genetic analyses support WG1 and GS3 function in a common pathway to control grain length. Thus, our findings reveal a previously unrecognized mechanism, in which redox regulation of a Gγ subunit by a glutaredoxin controls grain length, opening a novel perspective for G protein signaling regulation.