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    Low molecular weight protein tyrosine phosphatase (LWM-PTP), also known as acid phosphatase, is a highly conserved tyrosine phosphatase in living organisms. However, the function of LWM-PTP homolog has not been reported yet in plants. Here, we revealed a homolog of acid phosphatase, APH, in Arabidopsis plants, is a functional protein tyrosine phosphatase. The aph mutants are hyposensitive to ABA in post-germination growth. We performed an anti-phosphotyrosine antibody-based quantitative phosphoproteomics in wild-type and aph mutant and identified hundreds of putative targets of APH, including multiple splicing factors and other transcriptional regulators. Consistently, RNA-seq analysis revealed that the expression of ABA-highly-responsive genes is suppressed in aph mutants. Thus, APH regulates the ABA-responsive gene expressions by regulating the tyrosine phosphorylation of multiple splicing factors and other post-transcriptional regulators. We also revealed that Tyr383 in RAF9, a member of B2 and B3 RAF kinases that phosphorylate and activate SnRK2s in the ABA signaling pathway, is a direct target site of APH. Phosphorylation of Tyr383 is essential for RAF9 activity. Our results uncovered a crucial function of APH in ABA-induced tyrosine phosphorylation in Arabidopsis. The online version contains supplementary material available at 10.1007/s44154-022-00041-6. © The Author(s) 2022.


    Yanyan Du, Shaojun Xie, Yubei Wang, Yu Ma, Bei Jia, Xue Liu, Jingkai Rong, Rongxia Li, Xiaohong Zhu, Chun-Peng Song, W Andy Tao, Pengcheng Wang. Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis. Stress biology. 2022;2(1):23

    PMID: 35935594

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