A Novel Phosphatase Family, Structurally Related to Dual-specificity Phosphatases, that Displays Unique Amino Acid Sequence and Substrate Specificity

Romá-Mateo, Carlos; Ríos, Pablo; Tabernero, Lydia; Attwood, Teresa K.; Pulido, Rafael

doi:10.1016/j.jmb.2007.10.008

Cited by 19 publications

(37 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The A. thaliana genome encodes five isoforms of this protein, and S. cerevisiae has three isoforms (7,8). The structure of the A. thaliana AtPFA-DSP1 was determined by x-ray crystallography (21), and the yeast Siw14 ortholog was modeled based on this structure (7).…”

Section: Discussionmentioning

confidence: 99%

“…Two physiologically relevant isomers of IP 7 include 1PP-IP 5 and 5PP-IP 5 in which the pyrophosphate group is found at the 1-position or the 5-position, respectively. Sequential phosphorylation of IP 7 results in bisdiphosphoinositol tetrakisphosphate (1,5PP-IP 4 or IP 8 ) that is pyrophosphorylated at both the 1st and 5th positions (1,2). Since their discovery more than 20 years ago, inositol pyrophosphates have been implicated in an array of processes, including cellular energetic metabolism, telomere maintenance, oxidative stress response, and vesicle trafficking in animals and fungi (1).…”

mentioning

confidence: 99%

See 1 more Smart Citation

A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae

Steidle

Chong

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

Inositol pyrophosphates are high energy signaling molecules involved in cellular processes, such as energetic metabolism, telomere maintenance, stress responses, and vesicle trafficking, and can mediate protein phosphorylation. Although the inositol kinases underlying inositol pyrophosphate biosynthesis are well characterized, the phosphatases that selectively regulate their cellular pools are not fully described. The diphosphoinositol phosphate phosphohydrolase enzymes of the Nudix protein family have been demonstrated to dephosphorylate inositol pyrophosphates; however, the Saccharomyces cerevisiae homolog Ddp1 prefers inorganic polyphosphate over inositol pyrophosphates. We identified a novel phosphatase of the recently discovered atypical dual specificity phosphatase family as a physiological inositol pyrophosphate phosphatase. Purified recombinant Siw14 hydrolyzes the ␤-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP 5 or IP 7 ) in vitro. In vivo, siw14⌬ yeast mutants possess increased IP 7 levels, whereas heterologous SIW14 overexpression eliminates IP 7 from cells. IP 7 levels increased proportionately when siw14⌬ was combined with ddp1⌬ or vip1⌬, indicating independent activity by the enzymes encoded by these genes. We conclude that Siw14 is a physiological phosphatase that modulates inositol pyrophosphate metabolism by dephosphorylating the IP 7 isoform 5PP-IP 5 to IP 6 .Inositol pyrophosphates are a novel class of signaling molecules that carry energy-rich diphosphate bonds. In wild-type yeast, the most abundant isoform, diphosphoinositol pentakisphosphate (PP-IP 5 or IP 7 ), 5 consists of a fully phosphorylated six carbon myo-inositol ring further pyrophosphorylated at one of the carbons. Two physiologically relevant isomers of IP 7 include 1PP-IP 5 and 5PP-IP 5 in which the pyrophosphate group is found at the 1-position or the 5-position, respectively. Sequential phosphorylation of IP 7 results in bisdiphosphoinositol tetrakisphosphate (1,5PP-IP 4 or IP 8 ) that is pyrophosphorylated at both the 1st and 5th positions (1, 2). Since their discovery more than 20 years ago, inositol pyrophosphates have been implicated in an array of processes, including cellular energetic metabolism, telomere maintenance, oxidative stress response, and vesicle trafficking in animals and fungi (1). Recent work in Saccharomyces cerevisiae found that production of inositol pyrophosphates is essential for mounting environmental stress responses (3). Inositol pyrophosphates are thought to be metabolic regulators displaying expanded cellular roles beyond classic second messengers (1).The enzymes that regulate the pools of inositol pyrophosphates are not fully described. The inositol hexakisphosphate kinases synthesize IP 7 , the most abundant inositol pyrophosphate in the cell; they add the ␤-phosphate to IP 6 at the 5th position generating 5PP-IP 5 (2). Yeast possess a single inositol hexakisphosphate kinase gene, KCS1, whereas mammals possess three homologous genes encoding inositol hexakisphosphate kinase (Fig....

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae

Steidle

Chong

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…There are three types of lipid phosphatases in land plants: tumor suppressor phosphatase and tensin homologue deleted in chromosome 10 (PTEN), myotubular myopathy related protein (MTMR) and plant and fungi atypical dual-specificity phosphatase (PFA-DSP) (Roma-Mateo et al 2007). …”

Section: Introductionmentioning

confidence: 99%

“…The PFA-DSP lipid phosphatases have special substrate specificities for dephosphorylating phosphatidylinositol and comprise a subfamily of PTP that only exists in plants and fungi (Roma-Mateo et al 2007). AtPFA-DSP1 has displayed in vitro activity towards pyronitrophenyl phosphate (pNPP) and phosphoinositides.…”

Section: Introductionmentioning

confidence: 99%

OsPFA-DSP1, a rice protein tyrosine phosphatase, negatively regulates drought stress responses in transgenic tobacco and rice plants

et al. 2012

View full text Add to dashboard Cite

Dephosphorylation plays a pivotal role in regulating plant growth, development and abiotic/biotic stress responses. Here, we characterized a plant and fungi atypical dual-specificity phosphatase (PFA-DSP) subfamily member, OsPFA-DSP1, from rice. OsPFA-DSP1 was determined to be a functional protein tyrosine phosphatase (PTP) in vitro using phosphatase activity assays. Quantitative real-time PCR and GENEVESTIGATOR analysis showed that OsPFA-DSP1 mRNA was induced by drought stress. Transfection of rice protoplasts showed that OsPFA-DSP1 accumulated in both the cytoplasm and nucleus. Ectopic overexpression of OsPFA-DSP1 in tobacco increased sensitivity to drought stress and insensitivity to ABA-induced stomatal closure and inhibition of stomatal opening. Furthermore, overexpression of OsPFA-DSP1 in rice also increased sensitivity to drought stress. These results indicated that OsPFA-DSP1 is a functional PTP and may act as a negative regulator in drought stress responses.

show abstract

“…PFA-DSPs are a group of atypical DSPs present in plants and fungi. In Arabidopsis, there are five PFADSPs (Romá-Mateo et al, 2007. However, little is known about the function of PFA-DSPs, especially that of PFA-DSP5, in plants.…”

Section: Discussionmentioning

confidence: 99%

Histone H2B Monoubiquitination Is Involved in Regulating the Dynamics of Microtubules during the Defense Response to Verticillium dahliae Toxins in Arabidopsis

Pei

Zhang

et al. 2014

Plant Physiology

View full text Add to dashboard Cite

Histone H2B monoubiquitination (H2Bub) is being recognized as a regulatory mechanism that controls a range of cellular processes in plants, but the molecular mechanisms of H2Bub that are involved in responses to biotic stress are largely unknown. In this study, we used wild-type and H2Bub loss-of-function mutations of Arabidopsis (Arabidopsis thaliana) to elucidate which of its mechanisms are involved in the regulation of the plant's defense response to Verticillium dahliae (Vd) toxins. We demonstrate that the depolymerization of the cortical microtubules (MTs) was different in the wild type and the mutants in the response to Vd toxins. The loss-of-function alleles of HISTONE MONOUBIQUITINATION1 and HISTONE MONOUBIQUITINATION2 mutations present a weaker depolymerization of the MTs, and protein tyrosine phosphorylation plays a critical role in the regulation of the dynamics of MTs. Moreover, H2Bub is a positive regulator of the gene expression of protein tyrosine phosphatases. These findings provide direct evidence for H2Bub as an important modification with regulatory roles in the defense against Vd toxins and demonstrate that H2Bub is involved in modulating the dynamics of MTs, likely through the protein tyrosine phosphatase-mediated signaling pathway.

show abstract

A Novel Phosphatase Family, Structurally Related to Dual-specificity Phosphatases, that Displays Unique Amino Acid Sequence and Substrate Specificity

Cited by 19 publications

References 54 publications

A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae

A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae

OsPFA-DSP1, a rice protein tyrosine phosphatase, negatively regulates drought stress responses in transgenic tobacco and rice plants

Histone H2B Monoubiquitination Is Involved in Regulating the Dynamics of Microtubules during the Defense Response to Verticillium dahliae Toxins in Arabidopsis

Contact Info

Product

Resources

About