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A Phosphothreonine Residue at the C-Terminal End of the Plasma Membrane H+-ATPase Is Protected by Fusicoccin-Induced 14-3-3 Binding1

Anne Olsson*, Fredrik Svennelid, Bo Ek, Marianne Sommarin, and Christer Larsson

Department of Plant Biochemistry, Lund University, P.O. Box 117, SE-221 00 Lund, Sweden (A.O., F.S., M.S., C.L.); and Uppsala Genetic Center, Department of Plant Biology, Swedish University of Agricultural Sciences, P.O. Box 7080, SE-750 07 Uppsala, Sweden (B.E.)

We have isolated the plasma membrane H+-ATPase in a phosphorylated form from spinach (Spinacia oleracea L.) leaf tissue incubated with fusicoccin, a fungal toxin that induces irreversible binding of 14-3-3 protein to the C terminus of the H+-ATPase, thus activating H+ pumping. We have identified threonine-948, the second residue from the C-terminal end of the H+-ATPase, as the phosphorylated amino acid. Turnover of the phosphate group of phosphothreonine-948 was inhibited by 14-3-3 binding, suggesting that this residue may form part of a binding motif for 14-3-3. This is the first identification to our knowledge of an in vivo phosphorylation site in the plant plasma membrane H+-ATPase.

1   This work was supported by the Swedish Foundation for Strategic Research, the Swedish Natural Science Research Council, the Swedish Council for Forestry and Agricultural Research, and the European Union Biotechnology Program.
*   Corresponding author; anne.olsson{at}plantbio.lu.se; fax 46-462-224-116.

Plant Physiol. (1998) 118: 551-555
Copyright Clearance Center:   0032-0889/98/118//05
© 1998 American Society of Plant Physiologists




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