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Competitive binding of small antagonistic peptides to the OsER1 receptor optimizes rice architecture

文献类型： 外文期刊

作者： Guo, Tao 1 ; Si, Fuyan 1 ; Lu, Fei 1 ; Yang, Lianlian 1 ; Chen, Ke 3 ; Wang, Xiaopan 4 ; Li, Guanglin 4 ; Lu, Zi-Qi 2 ; Lin, Hong-Xuan 2 ;

作者机构： 1.Northwest A&F Univ, Inst Future Agr, Yangling 712100, Shaanxi, Peoples R China

2.Chinese Acad Sci, Natl Key Lab Plant Mol Genet, CAS Ctr Excellence Mol Plant Sci, Shanghai Inst Plant Physiol & Ecol, Shanghai 200032, Peoples R China

3.Guangdong Acad Agr Sci, Key Lab Genet & Breeding High Qual Rice Southern C, Minist Agr & Rural Affairs, Guangdong Rice Engn Lab,Rice Res Inst, Guangzhou 510640, Peoples R China

4.Shaanxi Normal Univ, Coll Life Sci, Natl Engn Lab Resource Dev Endangered Crude Drugs, Key Lab,Minist Educ Med Plant Resource & Nat Pharm, Xian 710119, Shaanxi, Peoples R China

关键词： rice; panicle architecture; antagonistic peptides; OsEPFL5; OsER1

期刊名称：PLANT COMMUNICATIONS （ 影响因子：11.6； 五年影响因子：11.8 ）

ISSN： 2590-3462

年卷期： 2025 年 6 卷 3 期

页码：

收录情况： SCI

摘要： Rice panicle architecture is a pivotal trait that strongly contributes to grain yield. Small peptide ligands from the OsEPF/EPFL family synergistically control panicle architecture by recognition of the OsER1 receptor and subsequent activation of the OsMKKK10-OsMKK4-OsMPK6 cascade, indicating that specific ligand-receptor pairs orchestrate rice panicle development. However, how small homologous peptides fine-tune organ morphogenesis by targeting a common receptor remains to be clarified. Here, we report that the small peptide OsEPFL5 acts as a ligand of the OsER1 receptor that inactivates the OsMKKK10- OsMKK4-OsMPK6 cascade, suggesting that OsEPFL5 plays a role opposite to that of the OsEPFL6/7/8/9 subfamily in regulating spikelet number per panicle and grain size. Notably, OsEPFL5 competitively replaces binding of OsEPFL6, OsEPFL7, OsEPFL8, or OsEPFL9 to the OsER1 receptor, revealing antagonistic competition between these small homologous peptides. Specifically enhancing the expression of OsEPFL5 can significantly improve grain yield by suppressing functions of the ligand-receptor pairs OsEPFL6- OsER1, OsEPFL7-OsER1, OsEPFL8-OsER1, and OsEPFL9-OsER1, suggesting that competitive binding to the OsER1 receptor by small antagonistic peptides can optimize rice panicle architecture. Our findings clarify how a receptor agonist and antagonist define inductive and inhibitory cues to shape rice panicle architecture, thus providing a new method for rationally breaking yield-trait coupling by manipulating small antagonistic peptides.

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