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J Biol Chem, Vol. 275, Issue 14, 9919-9923, April 7, 2000
From the The H+-ATPase is a key enzyme
for the establishment and maintenance of plasma membrane potential and
energization of secondary active transport in the plant cell. The
phytotoxin fusicoccin induces H+-ATPase activation by
promoting the association of 14-3-3 proteins. It is still unclear
whether 14-3-3 proteins can represent natural regulators of the proton
pump, and factors regulating 14-3-3 binding to the
H+-ATPase under physiological conditions are unknown as
well. In the present study in vivo and in vitro
evidence is provided that 14-3-3 proteins can associate with the
H+-ATPase from maize roots also in a fusicoccin-independent
manner and that the interaction depends on the phosphorylation status of the proton pump. Furthermore, results indicate that phosphorylation of H+-ATPase influences also the
fusicoccin-dependent interaction of 14-3-3 proteins.
Finally, a protein phosphatase 2A able to impair the interaction
between H+-ATPase and 14-3-3 proteins was identified and
partially purified from maize root.
Phosphorylation-dependent Interaction between Plant
Plasma Membrane H+-ATPase and 14-3-3 Proteins*
,,¶
Department of Biology, University of Rome
"Tor Vergata," via della Ricerca Scientifica, I-00133, Rome, Italy
and the § Department of Earth Sciences, University of
Sannio, via Port'Arsa 11, I-82100, Benevento, Italy
*
This work was supported in part by the National Research
Council (CNR Target Project on Biotechnology), by the Italian Ministry of University and Scientific Research, and by Contract BIO4-CT97-2275 of the European Union 4th Frame Biotechnology Program.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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