{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Du Y"],"funding":["Austrian Science Fund FWF","NIA NIH HHS","Medical Research Council","National Natural Science Foundation of China","National Institutes of Health","CYENS Centre of Excellence","Engineering and Physical Sciences Research Council"],"pagination":["23"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9345830"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2(1)"],"pubmed_abstract":["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> mut"],"journal":["Stress biology"],"pubmed_title":["Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis."],"pmcid":["PMC9345830"],"funding_grant_id":["P 22467","1675205","EP/P007619/1","RF1 AG064250","31771358","EP/N007050/1","739578","EP/D055466/1","3RF1AG064250","MR/S035540/1","EP/H046623/1","EP/S005927/1"],"pubmed_authors":["Liu X","Wang P","Song CP","Jia B","Tao WA","Ma Y","Du Y","Zhu X","Li R","Wang Y","Rong J","Xie S"],"additional_accession":[]},"is_claimable":false,"name":"Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis.","description":"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> mut","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-07-14T15:49:56.713Z","creation":"2025-02-19T05:06:18.386Z"},"accession":"S-EPMC9345830","cross_references":{"pubmed":["35935594"],"doi":["10.1007/s44154-022-00041-6"]}}