Protein tyrosine dephosphorylation during copper-induced cell death in rice roots

Hung, Wan Chi; Huang, Dinq Ding; Chien, Pei Shan; Yeh, Chuan Ming; Chen, Po‐Yu; Chang, Wen Chang; Huang, Hao

doi:10.1016/j.chemosphere.2007.04.073

Cited by 21 publications

(18 citation statements)

References 55 publications

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“…In parallel, a pharmacological approach using inhibitors specific to PTPs also revealed the importance of tyrosine dephosphorylation in physiological responses. For examples, treatment of rice roots with a PTP inhibitor (sodium orthovanadate) modulated copper-induced cell death (Hung et al 2007). ABA-dependent responses such as stomatal closure were modified by a PTP inhibitor (phenylarsine oxide), indicating the involvement of tyrosine dephosphorylation in ABA signaling (Ghelis et al 2008).…”

Section: Introductionmentioning

confidence: 99%

PaPTP1, a Gene Encoding Protein Tyrosine Phosphatase from Orchid, Phalaenopsis amabilis, is Regulated During Floral Development and Induced by Wounding

Lin

Kao

et al. 2010

Plant Mol Biol Rep

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Protein tyrosine phosphorylation is crucial in many cellular regulatory mechanisms, including development, stress management, and hormonal responses. However, the precise function of plant protein tyrosine phosphatase (PTP) has not been well elucidated. In this study, we report on the isolation and characterization of an orchid (Phalaenopsis amabilis) PTP gene, referred to as PaPTP1. The cloned PaPTP1 cDNA is 1,588 nucleotides long and the deduced protein sequence composed of 346 amino acid residues. The PaPTP1 gene encodes a classical plant PTP containing a catalytically active cysteine residue within the signature motif. Sequence homology analysis indicated that the predicted amino acid sequence is 57% identical to that of Arabidopsis AtPTP1. To our knowledge, the PaPTP1 is the first classical PTP identified in monocotyledon plant species. Southern blot analysis of genomic DNA revealed the presence of a single PaPTP1 gene in P. amabilis. Expression of PaPTP1 gene was examined in different organs of P. amabilis plants. The result showed that the PaPTP1 gene was abundantly expressed in labella and column of 24-month-old plants, but poorly in leaves. In addition, the PaPTP1 gene expression in response to wounding was investigated. The steady-state level of the PaPTP1 transcript increased significantly in wound-treated leaves. The identity as phosphatase was also demonstrated by characterizing the PaPTP1 expressed as a recombinant glutathione-Stransferase-fusion protein. The enzyme exhibited phosphatase activity towards a synthetic substrate, p-nitrophenolphosphate. Taken together, these results suggest that this PaPTP1 gene encodes a functional protein phosphatase, and its expression patterns are associated with the development of the orchid flowers and in response to wounding.

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Section: Introductionmentioning

confidence: 99%

PaPTP1, a Gene Encoding Protein Tyrosine Phosphatase from Orchid, Phalaenopsis amabilis, is Regulated During Floral Development and Induced by Wounding

Lin

Kao

et al. 2010

Plant Mol Biol Rep

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“…Tyr phosphorylated proteins have been detected in carrot (Daucus carota) cells, Mimosa pudica leaves, Arabidopsis hypocotyls, and Arabidopsis suspension cells (Barizza et al, 1999;Kameyama et al, 2000;Huang et al, 2003;Sugiyama et al, 2008). In addition, Tyr phosphorylation modulates embryogenesis in coconut (Cocos nucifera), and copper modulates Tyr phosphorylation of proteins in rice (Oryza sativa) roots (Islas-Flores et al, 1998;Hung et al, 2007). PTPs can be divided into two groups based on their phosphoamino acid specificity: Tyr-specific PTPs and dual-specificity PTPs (DsPTPs).…”

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confidence: 99%

Protein Tyrosine Kinases and Protein Tyrosine Phosphatases Are Involved in Abscisic Acid-Dependent Processes in Arabidopsis Seeds and Suspension Cells

et al. 2008

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Protein tyrosine (Tyr) phosphorylation plays a central role in many signaling pathways leading to cell growth and differentiation in animals. Tyr phosphorylated proteins have been detected in higher plants, and the roles of protein Tyr phosphatases and protein Tyr kinases in some physiological responses have been shown. We investigated the involvement of Tyr phosphorylation events in abscisic acid (ABA) signaling using a pharmacological approach. Phenylarsine oxide, a specific inhibitor of protein Tyr phosphatase activity, abolished the ABA-dependent accumulation of RAB18 (responsive to ABA 18) transcripts. Protein Tyr kinase inhibitors like genistein, tyrphostin A23, and erbstatin blocked the RAB18 expression induced by ABA in Arabidopsis (Arabidopsis thaliana). Stomatal closure induced by ABA was also inhibited by phenylarsine oxide and genistein. We studied the changes in the Tyr phosphorylation levels of proteins in Arabidopsis seeds after ABA treatment. Proteins were separated by two-dimensional gel electrophoresis, and those phosphorylated on Tyr residues were detected using an anti-phosphotyrosine antibody by western blot. Changes were detected in the Tyr phosphorylation levels of 19 proteins after ABA treatment. Genistein inhibited the ABA-dependent Tyr phosphorylation of proteins. The 19 proteins were analyzed by matrix-assisted laser-desorption ionization time-of-flight/time-of-flight mass spectrometry. Among the proteins identified were storage proteins like cruciferins, enzymes involved in the mobilization of lipid reserves like aconitase, enolase, aldolase, and a lipoprotein, and enzymes necessary for seedling development like the large subunit of Rubisco. Additionally, the identification of three putative signaling proteins, a peptidyl-prolyl isomerase, an RNA-binding protein, and a small ubiquitin-like modifier-conjugating enzyme, enlightens how Tyr phosphorylation might regulate ABA transduction pathways in plants.

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“…33,50,52 A PTP activity inhibited by dephostatin has been detected in soybean. 53 Using sodium ortho-vanadate, it has been shown that a PTP is implicated in the copper-dependent transduction pathway leading to cell death 34 and in the dynamics and organization of microtubules. 46 Once involved by these pharmacological approaches in several plant physiological processes, the genes encoding these enzymes were identified by analysis of the plant genomes using bioinformatics.…”

Section: Signal Processing By Protein Tyrosine Phosphorylation In Plantsmentioning

confidence: 99%

“…23 Immunoblotting with anti-phospho-Tyr antibodies have permitted detection of plant proteins phosphorylated on Tyr in several other species. 17,19,[24][25][26][27][28][29][30][31][32][33][34][35][36][37] Involvement of PTKs and PTPs by pharmacological approaches. One way to probe specifically elements of signal transduction pathways is by perturbating these pathways through the loss of function of one of these elements.…”

Section: Discovery Of Protein Tyrosine Phosphorylation and First Studmentioning

confidence: 99%

Signal processing by protein tyrosine phosphorylation in plants

Ghélis

2011

Plant Signaling & Behavior

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Protein tyrosine dephosphorylation during copper-induced cell death in rice roots

Cited by 21 publications

References 55 publications

PaPTP1, a Gene Encoding Protein Tyrosine Phosphatase from Orchid, Phalaenopsis amabilis, is Regulated During Floral Development and Induced by Wounding

PaPTP1, a Gene Encoding Protein Tyrosine Phosphatase from Orchid, Phalaenopsis amabilis, is Regulated During Floral Development and Induced by Wounding

Protein Tyrosine Kinases and Protein Tyrosine Phosphatases Are Involved in Abscisic Acid-Dependent Processes in Arabidopsis Seeds and Suspension Cells

Signal processing by protein tyrosine phosphorylation in plants

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