OsPRA2

• Symbol: OsPRA2
• MSU: LOC_Os06g50060
• RAPdb: Os06g0714600

• A Small G Protein as a Novel Component of the Rice Brassinosteroid Signal Transduction., 2016, Mol Plant.
• OsPRA2 fine-tunes rice brassinosteroid receptor., 2017, Plant Signal Behav.

Genbank accession number

• Lamina inclination, coleoptile elongation, and root inhibition assays indicated that rice plants with suppressed expression of OsPRA2 were more sensitive to exogenously applied brassinolide than wild-type plants
• Mechanistic study uncovered that OsPRA2 inhibited the dephosphorylation of, and thus inactivated the transcription factor BRASSINAZOLE-RESISTANT 1 (OsBZR1)
• More importantly, OsPRA2 was found to co-localize with and directly bind to rice BR receptor BRASSINOSTEROID-INSENSITIVE 1 (OsBRI1) on the plasma membrane
• Together, these results revealed a possible working mechanism of OsPRA2 as a novel negative regulator on OsBRI1 and OsBZR1 in the BR signaling pathway in rice, and further extended the knowledge about the regulatory mechanism of rice BR signaling
• OsPRA2 fine-tunes rice brassinosteroid receptor.
• Overexpression of OsGAP1 in Arabidopsis resulted in a phenotype mimic to BR-deficiency, implying that the GTPase activity of OsPRA2 is also involved in regulating BR signaling

• D61~OsBRI1~OsBRKq1~HFR131, OsPRA2, A Small G Protein as a Novel Component of the Rice Brassinosteroid Signal Transduction., More importantly, OsPRA2 was found to co-localize with and directly bind to rice BR receptor BRASSINOSTEROID-INSENSITIVE 1 (OsBRI1) on the plasma membrane
• D61~OsBRI1~OsBRKq1~HFR131, OsPRA2, A Small G Protein as a Novel Component of the Rice Brassinosteroid Signal Transduction., Together, these results revealed a possible working mechanism of OsPRA2 as a novel negative regulator on OsBRI1 and OsBZR1 in the BR signaling pathway in rice, and further extended the knowledge about the regulatory mechanism of rice BR signaling
• OsBZR1~BZR1, OsPRA2, A Small G Protein as a Novel Component of the Rice Brassinosteroid Signal Transduction., Mechanistic study uncovered that OsPRA2 inhibited the dephosphorylation of, and thus inactivated the transcription factor BRASSINAZOLE-RESISTANT 1 (OsBZR1)
• OsBZR1~BZR1, OsPRA2, A Small G Protein as a Novel Component of the Rice Brassinosteroid Signal Transduction., Together, these results revealed a possible working mechanism of OsPRA2 as a novel negative regulator on OsBRI1 and OsBZR1 in the BR signaling pathway in rice, and further extended the knowledge about the regulatory mechanism of rice BR signaling
• D61~OsBRI1~OsBRKq1~HFR131, OsPRA2, OsPRA2 fine-tunes rice brassinosteroid receptor., Recently we have reported that a rice small G protein, OsPRA2, bound to the BR receptor OsBRI1 at the plasma membrane (PM) and inhibited its kinase activity and its interaction with the co-receptor OsBAK1, leading to a lower sensitivity to BR treatment and dephosphorylation of OsBZR1
• D61~OsBRI1~OsBRKq1~HFR131, OsPRA2, OsPRA2 fine-tunes rice brassinosteroid receptor., In addition, we observed that, besides colocalizing at the PM, OsPRA2 was also colocalized with OsBRI1 in small granules near PM, suggesting that the function of OsPRA2 in vesicle traffic may contribute to the regulation of OsBRI1
• OsBISERK1~OsSERK1~OsBAK1~TBP1, OsPRA2, OsPRA2 fine-tunes rice brassinosteroid receptor., Recently we have reported that a rice small G protein, OsPRA2, bound to the BR receptor OsBRI1 at the plasma membrane (PM) and inhibited its kinase activity and its interaction with the co-receptor OsBAK1, leading to a lower sensitivity to BR treatment and dephosphorylation of OsBZR1
• OsBZR1~BZR1, OsPRA2, OsPRA2 fine-tunes rice brassinosteroid receptor., Recently we have reported that a rice small G protein, OsPRA2, bound to the BR receptor OsBRI1 at the plasma membrane (PM) and inhibited its kinase activity and its interaction with the co-receptor OsBAK1, leading to a lower sensitivity to BR treatment and dephosphorylation of OsBZR1
• OsGAP1, OsPRA2, OsPRA2 fine-tunes rice brassinosteroid receptor., Overexpression of OsGAP1 in Arabidopsis resulted in a phenotype mimic to BR-deficiency, implying that the GTPase activity of OsPRA2 is also involved in regulating BR signaling