Phosphorylation-dependent interaction between plant plasma membrane H+-ATPase and 14-3-3 proteins
Phosphorylation-dependent interaction between plant plasma membrane H+-ATPase and 14-3-3 proteins
复制标题
DOI：
10.1074/jbc.275.14.9919
复制
发表时间：
2000-04-07
影响因子：
4.8
通讯作者：
Aducci, P
中科院分区：
文献类型：
--
作者：
Camoni, L;Iori, V;Aducci, P
H ~+-ATP酶是植物细胞质膜电位的建立和维持以及次生主动运输的关键酶。植物毒素fusicoccin通过促进14-3-3蛋白的结合来诱导H+-ATPase活化。目前还不清楚14-3-3蛋白是否可以代表质子泵的天然调节剂，并且在生理条件下调节14-3-3与H+-ATP酶结合的因素也是未知的。在本研究中，在体内和体外的证据表明，14-3-3蛋白可以与H+-ATP酶从玉米根也在一个梭菌素独立的方式和相互作用取决于磷酸化状态的质子泵。此外，结果表明H+-ATP酶的磷酸化也影响14-3-3蛋白质的梭菌素依赖性相互作用。最后，从玉米根中鉴定并部分纯化了一种能够破坏H ~+-ATPase与14-3-3蛋白相互作用的蛋白磷酸酶2A。
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.