Rice LecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development.
J Exp Bot
; 71(14): 4033-4041, 2020 07 06.
Article
em En
| MEDLINE
| ID: mdl-32270203
ABSTRACT
The temporary callose layer surrounding the tetrads of microspores is critical for male gametophyte development in flowering plants, as abnormal callose deposition can lead to microspore abortion. A sophisticated signaling network regulates callose biosynthesis but these pathways are poorly understood. In this study, we characterized a rice male-sterile mutant, oslecrk5, which showed defective callose deposition during meiosis. OsLecRK5 encodes a plasma membrane-localized lectin receptor-like kinase, which can form a dimer with itself. Moreover, normal anther development requires the K-phosphorylation site (a conserved residue at the ATP-binding site) of OsLecRK5. In vitro assay showed that OsLecRK5 phosphorylates the callose synthesis enzyme UGP1, enhancing callose biosynthesis during anther development. Together, our results demonstrate that plasma membrane-localized OsLecRK5 phosphorylates UGP1 and promotes its activity in callose biosynthesis in rice. This is the first evidence that a receptor-like kinase positively regulates callose biosynthesis.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oryza
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article