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Plant and Cell Physiology, 2002, Vol. 43, No. 11 1359-1365
© 2002 Oxford University Press

Biochemical Evidence for the Requirement of 14-3-3 Protein Binding in Activation of the Guard-cell Plasma Membrane H+-ATPase by Blue Light

Toshinori Kinoshita and Ken-ichiro Shimazaki1

Department of Biology, Faculty of Sciences, Kyushu University, Ropponmatsu, Fukuoka, 810-8560 Japan

Blue light (BL) activates the plasma membrane H+-ATPase via phosphorylation of the C-terminus with concomitant binding of 14-3-3 protein to the terminus in stomatal guard cells. However, the binding site and role of 14-3-3 protein in this physiological response have not been elucidated. We investigated the above using synthetic phosphopeptides designed from the C-terminus of Vicia H+-ATPase (isoform 1; VHA1). The presence of KGLDIDTIQQHYphospho-T950V peptide (P-950) prevented binding of 14-3-3 protein to the phosphorylated H+-ATPase. Dephosphorylated P-950 and other phosphopeptides, including typical phosphorylation sites in the C-terminus, had no effect on the binding. Incubation of BL-activated plasma membrane H+-ATPase with P-950 dissociated the 14-3-3 protein from the H+-ATPase without affecting phosphorylation levels and decreased the H+-ATPase activity. By contrast, incubation of P-950 with the activated H+-ATPase from fusicoccin-treated guard-cell protoplasts neither dissociated the 14-3-3 protein nor decreased the H+-ATPase activity. These results indicate that BL induces phosphorylation on threonine residue (Thr950) in the C-terminus of H+-ATPase, and that the binding of 14-3-3 to this site is required for the activation of H+-ATPase in stomatal guard cells.

1 Corresponding author: E-mail, kenrcb@mbox.nc.kyushu-u.ac.jp; Fax, +81-92-726-4758.


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