- Information
- Symbol: OsLecRK-S.7,OsLecRK5,OsDAF1
- MSU: LOC_Os02g26160
- RAPdb: Os02g0459600
- Publication
- Lectin receptor kinase OsLecRK-S.7 is required for pollen development and male fertility., 2019, J Integr Plant Biol.
- Rice OsLecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development., 2020, J Exp Bot.
- Rice pollen aperture formation is regulated by the interplay between OsINP1 and OsDAF1., 2020, Nat Plants.
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Genbank accession number
- Key message
- Lectin receptor kinase OsLecRK-S.7 is required for pollen development and male fertility.
- Rice OsLecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development.
- 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
- OsLecRK5 encodes a plasma membrane (PM)-localized lectin receptor like kinase, which can form dimer with itself
- Connection
- OsLecRK-S.7~OsLecRK5~OsDAF1, OsUgp1~Ugp1~UGPase1, Rice OsLecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development., In vitro assay showed that OsLecRK5 phosphorylates the callose synthesis enzyme UGP1, enhancing callose biosynthesis during anther development
- OsLecRK-S.7~OsLecRK5~OsDAF1, OsUgp1~Ugp1~UGPase1, Rice OsLecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development., Together, our results demonstrated that PM-localized OsLecRK5 phosphorylates UGP1 and promotes its activity in callose biosynthesis in rice
- OsINP1, OsLecRK-S.7~OsLecRK5~OsDAF1, Rice pollen aperture formation is regulated by the interplay between OsINP1 and OsDAF1., Rice pollen aperture formation is regulated by the interplay between OsINP1 and OsDAF1.
- OsINP1, OsLecRK-S.7~OsLecRK5~OsDAF1, Rice pollen aperture formation is regulated by the interplay between OsINP1 and OsDAF1., Furthermore, our results demonstrate that OsINP1 is required for polarization of OsDAF1 via direct protein interaction, suggesting that OsINP1 has an additional role in the formation of annulus that is absent in Arabidopsis
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