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. 2021 Dec 2;16(12):2000808.
doi: 10.1080/15592324.2021.2000808. Epub 2021 Nov 28.

AtPFA-DSP5 interacts with MPK3/MPK6 and negatively regulates plant salt responses

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AtPFA-DSP5 interacts with MPK3/MPK6 and negatively regulates plant salt responses

Jing Xin et al. Plant Signal Behav. .

Abstract

Protein tyrosine phosphatases play essential roles in plant growth and development and in plant responses to biotic or abiotic stresses. We recently demonstrated that an atypical dual-specificity protein tyrosine phosphatase in plants, AtPFA-DSP3 (DSP3), negatively regulates plant salt tolerance. Here, we report that a homolog of DSP3, AtPFA-DSP5 (DSP5), affects the response of plants to high-salt conditions. A loss-of-function mutant of DSP5 showed reduced sensitivity to salt treatment at the seed germination and vegetative stages of development while a gain-of-function mutant of DSP5 showed increased sensitivity to salt stress. The salt responses of dsp3dsp5 double-mutant plants were similar to those of dsp3 and dsp5 single-mutant plants. Gel overlay and firefly luciferase complementation assays showed that DSP5 interacts with MPK3 and MPK6 in vitro and in vivo. These results indicate that DSP5 is a novel negative regulator of salt responses in Arabidopsis that interacts directly with MPK3 and MPK6.

Keywords: Arabidopsis; AtPFA-DSP5; protein tyrosine phosphatase; salt stress.

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Conflict of interest statement

No potential conflict of interest was reported by the author(s).

Figures

Figure 1.
Figure 1.
The mutation of DSP5 confers salt tolerance in Arabidopsis.
Figure 2.
Figure 2.
The dsp5 mutant shows reduced sensitivity to KCl and mannitol.
Figure 3.
Figure 3.
The phenotype of salt-treated dsp3dsp5 double mutant plants.
Figure 4.
Figure 4.
DSP5 interacts with MPK3/MPK6.

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This work was supported by the National Science Foundation of China (Grant Nos. 31501151 and 31872830) and the Department of Education of Hebei Province (Grant No. BJ2019025).

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