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

被引:78
作者
Camoni, L
Iori, V
Marra, M
Aducci, P
机构
[1] Univ Roma Tor Vergata, Dept Biol, I-00133 Rome, Italy
[2] Univ Sannio, Dept Earth Sci, I-82100 Benevento, Italy
关键词
D O I
10.1074/jbc.275.14.9919
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:9919 / 9923
页数:5
相关论文
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