ArticleMolecular genetics and genomics : MGG2011
Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms.
Article in Molecular genetics and genomics : MGG, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 31 citations in OpenAlex.
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
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- Bridging Manual and Computational Approaches: The Pseudophosphatase Scanner for Genome-Wide Fungal Pseudophosphatome Analysis.ACS omega · 2026Article
- Expression, Purification, and Preliminary Characterization of Putative Protein Tyrosine Phosphatase Oca1.Protein and peptide letters · 2025Article
- Article
- AtPFA-DSP5 interacts with MPK3/MPK6 and negatively regulates plant salt responses.Plant signaling & behavior · 2021Article
- Investigation of RNA metabolism through large-scale genetic interaction profiling in yeast.Nucleic acids research · 2021Article
- Importance of tyrosine phosphorylation for transmembrane signaling in plants.The Biochemical journal · 2021Review
- Structural and biochemical characterization of Siw14: A protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates.The Journal of biological chemistry · 2018Article
- High-density ddRAD linkage and yield-related QTL mapping delimits a chromosomal region responsible for oil content in rapeseed (Breeding science · 2017Article
- A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae: Siw14 PROTEIN SELECTIVELY CLEAVES THE β-PHOSPHATE FROM 5-DIPHOSPHOINOSITOL PENTAKISPHOSPHATE (5PP-IP5).The Journal of biological chemistry · 2016Article
- The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Antioxidants & redox signaling · 2014Review
- Histone H2B monoubiquitination is involved in regulating the dynamics of microtubules during the defense response to Verticillium dahliae toxins in Arabidopsis.Plant physiology · 2014Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Dual-specificity phosphatases (DSPs) constitute a large protein tyrosine phosphatase (PTP) family, with examples in distant evolutive phyla. PFA-DSPs (Plant and Fungi Atypical DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds, the members of which share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The analysis of the PFA-DSPs from the plant Arabidopsis thaliana (AtPFA-DSPs) showed differential tissue mRNA expression, substrate specificity, and catalytic activity for these proteins, suggesting different functional roles among plant PFA-DSPs. Bioinformatic analysis revealed the existence of novel PFA-DSP-related proteins in fungi (Oca1, Oca2, Oca4 and Oca6 in Saccharomyces cerevisiae) and protozoa, which were segregated from plant PFA-DSPs. The closest yeast homolog for these proteins was the PFA-DSP from S. cerevisiae ScPFA-DSP1/Siw14/Oca3. Oca1, Oca2, Siw14/Oca3, Oca4, and Oca6 were involved in the yeast response to caffeine and rapamycin stresses. Siw14/Oca3 was an active phosphatase in vitro, whereas no phosphatase activity could be detected for Oca1. Remarkably, overexpression of Siw14/Oca3 suppressed the caffeine sensitivity of oca1, oca2, oca4, and oca6 deleted strains, indicating a genetic linkage and suggesting a functional relationship for these proteins. Functional studies on mutations targeting putative catalytic residues from the A. thaliana AtPFA-DSP1/At1g05000 protein indicated the absence of canonical amino acids acting as the general acid/base in the phosphor-ester hydrolysis, which suggests a specific mechanism of reaction for PFA-DSPs and related enzymes. Our studies demonstrate the existence of novel phosphatase protein families in fungi and protozoa, with active and inactive enzymes linked in common signaling pathways. This illustrates the catalytic and functional complexity of the expanding family of atypical dual-specificity phosphatases in non-metazoans, including parasite organisms responsible for infectious human diseases.
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