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 143-3 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.

Camoni, L., Iori, V., Marra, M., Aducci, P. (2000). Phosphorylation-dependent interaction between plant plasma membrane H+- ATPase and 14-3-3 proteins. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 275(14), 9919-9923 [10.1074/jbc.275.14.9919].

Phosphorylation-dependent interaction between plant plasma membrane H+- ATPase and 14-3-3 proteins

CAMONI, LORENZO;MARRA, MAURO;ADUCCI, PATRIZIA
2000-01-01

Abstract

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 143-3 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.
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Rilevanza internazionale
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Sì, ma tipo non specificato
Settore BIO/04
English
Con Impact Factor ISI
Camoni, L., Iori, V., Marra, M., Aducci, P. (2000). Phosphorylation-dependent interaction between plant plasma membrane H+- ATPase and 14-3-3 proteins. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 275(14), 9919-9923 [10.1074/jbc.275.14.9919].
Camoni, L; Iori, V; Marra, M; Aducci, P
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/41248
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