AtPFA‐DSP3, an atypical dual‐specificity protein tyrosine phosphatase, affects salt stress response by modulating MPK3 and MPK6 activity

• DOI: 10.1111/pce.14002
• Publication Date: 2021-01-19T18:22:27Z
• Authors: Jing Xin; Chuanling Li; Kexin Ning; Yuan Qin; Jian‐Xiu Shang; Yu Sun
• Keywords: Dual-specificity phosphatase

Protein phosphorylation, especially serine/threonine and tyrosine plays significant roles in signalling during plant growth development as well responses to biotic or abiotic stresses. Dual-specificity protein phosphatases dephosphorylate components of these pathways. Here, we report that an atypical dual-specificity phosphatase, AtPFA-DSP3 (DSP3), negatively affects the response plants high-salt conditions. A DSP3 loss-of-function mutant showed reduced sensitivity salt treatment. was primarily localized nuclei degraded Compared wild type, level ROS lower dsp3 higher ectopically expressing DSP3, indicating associated with increased production. interacted dephosphorylated MPK3 MPK6. Genetic analyses a dsp3mpk3 double revealed DSP3's effect on stress depends MPK3. Moreover, phosphatase activity required for its role signalling. These results indicate is negative regulator Arabidopsis by directly modulating accumulation phosphorylated