ArticleThe Plant cell2024
A transthyretin-like protein acts downstream of miR397 and LACCASE to regulate grain yield in rice.
Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- RNA regulation in plants.Science China. Life sciences · 2026Review
- Copper-sensitive OsSPL9 TF regulates expression of indica rice domestication-associated miRNAs and phenotypes.Communications biology · 2026Article
- Recent advances in miRNAs mediated agronomical advantageous traits improvement in rice.Molecular biology reports · 2026Review
- MicroRNA networks in rice seeds: unveiling key regulators of development, germination, and rice resilience under climate changes.Journal of experimental botany · 2026Review
- Genome-wide identification, classification and expression analysis of laccase family members in Solanum lycopersicum.BMC plant biology · 2026Article
- Auxin meets BR: OsIAA7 teams up with OsGSK2 to destabilize OsBZR1 for rice seed size control.The Plant cell · 2025Article
- Integrative analyses reveal Bna-miR397a-BnaLAC2 as a potential modulator of low-temperature adaptability in Brassica napus L.Plant biotechnology journal · 2025Article
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Authors and funding
11 authors.
Funding
Abstract
Increasing grain yield is a major goal of breeders due to the rising global demand for food. We previously reported that the miR397-LACCASE (OsLAC) module regulates brassinosteroid (BR) signaling and grain yield in rice (Oryza sativa). However, the precise roles of laccase enzymes in the BR pathway remain unclear. Here, we report that OsLAC controls grain yield by preventing the turnover of TRANSTHYRETIN-LIKE (OsTTL), a negative regulator of BR signaling. Overexpressing OsTTL decreased BR sensitivity in rice, while loss-of-function of OsTTL led to enhanced BR signaling and increased grain yield. OsLAC directly binds to OsTTL and regulates its phosphorylation-mediated turnover. The phosphorylation site Ser226 of OsTTL is essential for its ubiquitination and degradation. Overexpressing the dephosphorylation-mimic form of OsTTL (OsTTLS226A) resulted in more severe defects than did overexpressing OsTTL. These findings provide insight into the role of an ancient laccase in BR signaling and suggest that the OsLAC-OsTTL module could serve as a target for improving grain yield.
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Registered trials
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