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J Biol Chem, Vol. 274, Issue 51, 36774-36780, December 17, 1999
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From the 14-3-3 proteins play a regulatory role in a
diverse array of cellular functions such as apoptosis, regulation of
the cell cycle, and regulation of gene transcription. The phytotoxin
fusicoccin specifically induces association of virtually any 14-3-3 protein to plant plasma membrane H+-ATPase. The
14-3-3 binding site in the Arabidopsis plasma membrane H+-ATPase AHA2 was localized to the three C-terminal
residues of the enzyme (Tyr946-Thr-Val). Binding of 14-3-3 protein to this target was induced by phosphorylation of
Thr947 (KD = 88 nM) and
was in practice irreversible in the presence of fusicoccin
(KD = 7 nM). Mass spectrometry
analysis demonstrated that AHA2 expressed in yeast was phosphorylated
at Thr947. We conclude that the extreme end of AHA2
contains an unusual high-affinity binding site for 14-3-3 protein.
Department of Plant Biology, Royal
Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871
Frederiksberg, Copenhagen, Denmark, the ¶ Department of Biology,
University of Rome "Tor Vergata," via della Ricerca
Scientifica, 00133 Rome, Italy, the Protein Research Group,
Department of Molecular Biology, Odense University/University of
Southern Denmark, DK-5230 Odense M., Denmark, and the ** Department of
Plant Biology, University of Rome "La Sapienza," P. le A. Moro 5, 00185 Rome, Italy
To whom correspondence should be addressed. Tel.: 45-3528-2592;
Fax: 45-3528-3333; E-mail: palmgren@biobase.dk.
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