biostudies-literatureDu YAustrian Science Fund FWFNIA NIH HHSMedical Research CouncilNational Natural Science Foundation of ChinaNational Institutes of HealthCYENS Centre of ExcellenceEngineering and Physical Sciences Research Council23https://www.ebi.ac.uk/biostudies/studies/S-EPMC9345830biostudies-literatureUnknown2(1)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 <i>aph</i> mutants are hyposensitive to ABA in post-germination growth. We performed an anti-phosphotyrosine antibody-based quantitative phosphoproteomics in wild-type and <i>aph</i> 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 <i>aph</i> mutStress biologyLow molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis.PMC9345830P 224671675205EP/P007619/1RF1 AG06425031771358EP/N007050/1739578EP/D055466/13RF1AG064250MR/S035540/1EP/H046623/1EP/S005927/1Liu XWang PSong CPJia BTao WAMa YDu YZhu XLi RWang YRong JXie SfalseLow 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 <i>aph</i> mutants are hyposensitive to ABA in post-germination growth. We performed an anti-phosphotyrosine antibody-based quantitative phosphoproteomics in wild-type and <i>aph</i> 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 <i>aph</i> mut2022-01-01T00:00:00Z20222026-07-14T15:49:56.713Z2025-02-19T05:06:18.386ZS-EPMC93458303593559410.1007/s44154-022-00041-6