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Oscillating Aquaporin Phosphorylation and 14-3-3 Proteins Mediate the Circadian Regulation of Leaf Hydraulics

文献类型： 外文期刊

作者： Prado, Karine 1 ; Cotelle, Valerie 2 ; Li, Guowei 1 ; Bellati, Jorge 1 ; Tang, Ning 1 ; Tournaire-Roux, Colette 1 ; Ma 1 ;

作者机构： 1.Univ Montpellier, Montpellier SupAgro, INRA, Biochim & Physiol Mol Plantes,CNRS, F-34090 Montpellier, France

2.Univ Toulouse, Lab Rech Sci Vegetales, CNRS, UPS, 24 Chemin Borde Rouge,BP 42617, F-31326 Castanet Tolosan, France

3.Carnegie Inst Sci, Dept Plant Biol, 290 Panama St, Stanford, CA 94305 USA

4.Shandong Acad Agr Sci, Biotech Res Ctr, Shandong Prov Key Lab Crop Genet Improvement Ecol, Jinan 250100, Shandong, Peoples R China

期刊名称：PLANT CELL （ 影响因子：11.277； 五年影响因子：12.061 ）

ISSN： 1040-4651

年卷期： 2019 年 31 卷 2 期

页码：

收录情况： SCI

摘要： The circadian clock regulates plant tissue hydraulics to synchronize water supply with environmental cycles and thereby optimize growth. The circadian fluctuations in aquaporin transcript abundance suggest that aquaporin water channels play a role in these processes. Here, we show that hydraulic conductivity (K-ros) of Arabidopsis (Arabidopsis thaliana) rosettes displays a genuine circadian rhythmicity with a peak around midday. Combined immunological and proteomic approaches revealed that phosphorylation at two C-terminal sites (Ser280, Ser283) of PLASMA MEMBRANE INTRINSIC PROTEIN 2;1 (AtPIP2;1), a major plasma membrane aquaporin in rosettes, shows circadian oscillations and is correlated with K-ros. Transgenic expression of phosphodeficient and phosphomimetic forms of this aquaporin indicated that AtPIP2;1 phosphorylation is necessary but not sufficient for K-ros regulation. We investigated the supporting role of 14-3-3 proteins, which are known to interact with and regulate phosphorylated proteins. Individual knockout plants for five 14-3-3 protein isoforms expressed in rosettes lacked circadian activation of K-ros. Two of these [GRF4 (14-3-3Phi); GRF10 (14-3-3Epsilon)] showed direct interactions with AtPIP2;1 in the plant and upon coexpression in Xenopus laevis oocytes and activated AtPIP2;1, preferentially when the latter was phosphorylated at its two C-terminal sites. We propose that this regulatory mechanism assists in the activation of phosphorylated AtPIP2;1 during circadian regulation of K-ros.

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