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Literature summary for 1.6.3.1 extracted from

  • Ogasawara, Y.; Kaya, H.; Hiraoka, G.; Yumoto, F.; Kimura, S.; Kadota, Y.; Hishinuma, H.; Senzaki, E.; Yamagoe, S.; Nagata, K.; Nara, M.; Suzuki, K.; Tanokura, M.; Kuchitsu, K.
    Synergistic activation of the Arabidopsis NADPH oxidase AtrbohD by Ca2+ and phosphorylation (2008), J. Biol. Chem., 283, 8885-8892.
    View publication on PubMed
Search for more literature for 1.6.3.1

Activating Compound

Activating Compound Comment Organism Structure
calyculin isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin. Calyculin itself induces reactive oxygen species production and dramatically enhances the ionomycin-induced reactive oxygen species production of isoform RbohD Arabidopsis thaliana
ionomycin reactive oxygen species production by isoform RbohD is induced in presence of ionomycin. Ionomycin induces calcium influx into the cell, and following Ca2+ binding to the EF-hand motif of RbohD, conformational changes result in activation Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9FIJ0 isoform RbohD
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining