Dataset Information

Involvement of low molecular weight tyrosine acid phosphatase in abscisic acid signaling in Arabidopsis

ABSTRACT: Low molecular weight protein tyrosine phosphatase (LWM-PTP) is highly conserved tyrosine phosphatase from plants to animals. The function and putative targets of plant LWM-PTP homolog is not reported yet. Here, we revealed that Arabidopsis LWM-PTP homolog APH is a functional tyrosine phosphatase. APH participates in ABA signaling and regulates the ABA-responsive genes by regulates the tyrosine phosphorylation of multiple splicing factors and other transcriptional regulators. APH may also target RAF9, a member of B2 and B3 RAF kinases that activates SnRK2s, the key components in ABA-receptor coupled core signaling pathway. We preformed genetic analysis and found the aph mutants are hyposensitive to ABA in post-germination growth. We also performed an anti-phosphotyrosine antibody-based phosphoproteomics and studied the global change of phosphotyrosine in response to the ABA and APH. Hundreds of proteins, include SR45 and RAF9, are identified putative targets of APH. Consistent with it, aph mutants showed an ABA hyposensitive phenotype and altered expression of ABA-highly-responsive genes. Our results reveal a crucial function of APH in regulating tyrosine phosphorylation and ABA signaling in model plant Arabidopsis.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

DISEASE(S): Disease Free

SUBMITTER: Rongxia Li

LAB HEAD: Pengcheng Wang

PROVIDER: PXD029650 | Pride | 2022-10-14

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20170210_F_lrx_HCC-KD-ABA1.raw	Raw
	20170210_F_lrx_HCC-KD-ABA2.raw	Raw
	20170210_F_lrx_HCC-KD-ABA3.raw	Raw
	20170210_F_lrx_HCC-KD-con1.raw	Raw
	20170210_F_lrx_HCC-KD-con2.raw	Raw

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Publications

Low molecular weight protein phosphatase APH mediates tyrosine dephosphorylation and ABA response in Arabidopsis.

Du Yanyan Y Xie Shaojun S Wang Yubei Y Ma Yu Y Jia Bei B Liu Xue X Rong Jingkai J Li Rongxia R Zhu Xiaohong X Song Chun-Peng CP Tao W Andy WA Wang Pengcheng P

Stress biology 20220518 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 p ...[more]

PMID: 35935594

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Project description:Vascular endothelial protein tyrosine phosphatase (VE-PTP, PTPRB) is a receptor type phosphatase that is crucial for the regulation of endothelial junctions and blood vessel development. VE-PTP regulates vascular integrity by dephosphorylating substrates which are key players in endothelial junction stability, such as the angiopoietin receptor TIE2, the endothelial adherens junction protein VE-cadherin and the vascular endothelial growth factor receptor VEGFR2. Here, we have systematically searched for novel substrates of VE-PTP in endothelial cells by utilizing two approaches. First, we studied changes in the endothelial phosphoproteome upon exposing cells to a highly VE-PTP-specific phosphatase inhibitor followed by affinity isolation and mass-spectrometric analysis of phosphorylated proteins by phosphotyrosine-specific antibodies. Second, we used a substrate trapping mutant of VE-PTP to pull down phosphorylated substrates in combination with SILAC-based quantitative mass spectrometry measurements. We identified a set of substrate candidates of VE-PTP, of which a remarkably large fraction is related to cell junctions (48/165; 29.1%). Several of those were found in both screens and displayed very high connectivity in predicted functional interaction networks. The receptor protein tyrosine kinase EPHB4 was the most prominently phosphorylated protein upon VE-PTP inhibition among those VE-PTP targets that were identified by both proteomic approaches. Further analysis revealed that EPHB4 forms a ternary complex with VE-PTP and TIE2 in endothelial cells. VE-PTP controls the phosphorylation of each of these two tyrosine kinase receptors. Despite of their simultaneous presence in a ternary complex, stimulating each of the receptors with their own specific ligand did not cross-activate the respective partner receptor. Our systematic approach has led to the identification of novel substrates of VE-PTP, of which many are relevant for the control of cellular junctions further promoting the importance of VE-PTP as a key player of junctional signalling.