Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis.
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.
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.
Abscisic acid / tyrosine phosphorylaiton / phosphatase / kinase / phosphoproteomics / transcriptional regulation / RAF / SnRK2
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