broad bean (Vicia faba) phototropins (Vfphots)
First-pass extracted concept
Vicia faba phototropins
Aliases
Vfphot1a, Vfphot1b, Vfphots
Evidence Snippets
Supporting Sources
Linked Claims
A 14-3-3 protein binds to Vicia faba phototropins upon phosphorylation.
We found that a 14-3-3 protein was bound to Vfphots upon phosphorylation
Vicia faba phototropins act as blue-light receptors in guard cells.
We conclude that Vfphots act as BL receptors in guard cells
Blue-light-induced binding of a 14-3-3 protein to phototropin also occurs in etiolated seedlings and leaves, suggesting it is common to phototropin-mediated responses.
The binding of a 14-3-3 protein to Vfphot was found in etiolated seedlings and leaves in response to BL, suggesting that this event was common to phototropin-mediated responses.
Phosphorylation of a serine residue between LOV1 and LOV2 followed by 14-3-3 protein binding is likely to be a key step in the blue-light response in stomata.
phosphorylation of a Ser residue between LOV1 and LOV2 and subsequent 14-3-3 protein binding are likely to be key steps of BL response in stomata
Blue light induces phosphorylation of Vicia faba phototropins in guard cell protoplasts.
Using guard cell protoplasts, we showed that broad bean (Vicia faba) phototropins (Vfphots) were phosphorylated by BL
The phosphorylation sites identified for Vfphot1a and Vfphot1b are Ser-358 and Ser-344, respectively, located between LOV1 and LOV2.
phosphorylation sites were determined to be Ser-358 for Vfphot1a and Ser-344 for Vfphot1b, which are localized between LOV1 and LOV2
Phosphorylation of Vicia faba phototropins reaches its maximum earlier than phosphorylation of the H+-ATPase.
this phosphorylation of Vfphots reached to the maximum level earlier than that of the H+-ATPase