Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr946-Thr-Val and requires phosphorylation of Thr947
Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr946-Thr-Val and requires phosphorylation of Thr947
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DOI：
10.1074/jbc.274.51.36774
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发表时间：
1999-12-17
影响因子：
4.8
通讯作者：
Palmgren, MG
中科院分区：
文献类型：
--
作者：
Fuglsang, AT;Visconti, S;Palmgren, MG
14-3-3蛋白在多种细胞功能如凋亡、细胞周期调节和基因转录调节中起调节作用。植物毒素fusicoccin特异性地诱导几乎任何14-3-3蛋白与植物质膜Hf-ATPase的结合。拟南芥质膜H+-ATPase AHA 2的14-3-3结合位点定位于该酶的三个C-末端残基（Tyr（946）-Thr-Val）。通过Thr（947）的磷酸化（K-D = 88 nM）诱导14-3-3蛋白质与该靶点的结合，并且实际上在梭孢菌素（K-D = 7 nM）存在下是不可逆的。质谱分析表明，在酵母中表达的AHA 2在Thr（947）处被磷酸化。我们的结论是，AHA 2的极端末端包含一个不寻常的高亲和力结合位点的14-3-3蛋白。
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 Hf-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 (Tyr(946)-Thr-Val). finding of 14-3-3 protein to this target was induced by phosphorylation of Thr(947) (K-D = 88 nM) and was in practice irreversible in the presence of fusicoccin (K-D = 7 nM). Mass spectrometry analysis demonstrated that AHA2 expressed in yeast was phosphorylated at Thr(947). We conclude that the extreme end of AHA2 contains an unusual high-affinity binding site for 14-3-3 protein.