Mechanistic aspects of the low-molecular-weight phosphatase activity of calcineurin: a model for phosphotyrosyl-protein phosphatases

Martin, Bruce L.

doi:10.31274/rtd-180813-17367

Cited by 3 publications

(3 citation statements)

References 108 publications

(134 reference statements)

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“…Several kinetic and chemical data, available for calcineurin, support also for the Ser/Thr protein phosphatases a mechanism with a direct phosphoryl-group transfer to water (Martin & Graves, 1986, 1994. The importance of His151 for catalysis (corresponding to His202 in kbPAP) has been shown by mutational analysis on the bacteriophage l PP, revealing a decrease in k cat by a factor of 10 5 (Zhuo et al, 1994).…”

Section: Comparison To the Ser/thr Protein Phosphatasesmentioning

confidence: 99%

Mechanism of Fe(III) – Zn(II) Purple Acid Phosphatase Based on Crystal Structures

Klabunde

Sträter

Fröhlich

et al. 1996

Journal of Molecular Biology

353

450

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Section: Comparison To the Ser/thr Protein Phosphatasesmentioning

confidence: 99%

Mechanism of Fe(III) – Zn(II) Purple Acid Phosphatase Based on Crystal Structures

Klabunde

Sträter

Fröhlich

et al. 1996

Journal of Molecular Biology

353

450

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“…In support of this hypothesis, it has previously been reported that Pi plays a role in phosphorylation of NKA [341] and high concentrations of Pi inhibit enzyme activity [342]. Furthermore, previous studies have also shown that Pi inhibits phosphatase activity of calcineurin (Cn) [343]. As previously described, dephosphorylation of NKA is mediated by Cn [2].…”

Section: Molecular Mechanisms By Which Fluoride Inhibits Na+ K+-amentioning

confidence: 64%

Fluoride Exposure Induces Inhibition of Sodium-and Potassium-Activated Adenosine Triphosphatase (Na+, K+-ATPase) Enzyme Activity: Molecular Mechanisms and Implications for Public Health

Waugh¹

2019

IJERPH

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In this study, several lines of evidence are provided to show that Na + , K + -ATPase activity exerts vital roles in normal brain development and function and that loss of enzyme activity is implicated in neurodevelopmental, neuropsychiatric and neurodegenerative disorders, as well as increased risk of cancer, metabolic, pulmonary and cardiovascular disease. Evidence is presented to show that fluoride (F) inhibits Na + , K + -ATPase activity by altering biological pathways through modifying the expression of genes and the activity of glycolytic enzymes, metalloenzymes, hormones, proteins, neuropeptides and cytokines, as well as biological interface interactions that rely on the bioavailability of chemical elements magnesium and manganese to modulate ATP and Na + , K + -ATPase enzyme activity. Taken together, the findings of this study provide unprecedented insights into the molecular mechanisms and biological pathways by which F inhibits Na + , K + -ATPase activity and contributes to the etiology and pathophysiology of diseases associated with impairment of this essential enzyme. Moreover, the findings of this study further suggest that there are windows of susceptibility over the life course where chronic F exposure in pregnancy and early infancy may impair Na + , K + -ATPase activity with both short- and long-term implications for disease and inequalities in health. These findings would warrant considerable attention and potential intervention, not to mention additional research on the potential effects of F intake in contributing to chronic disease.

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“…Several immunosuppressant drugs have been reported to inhibit the activity of CaN . The biological roles of CaN have become more comprehensive with the elucidation of its three‐dimensional structure . However, the function of insect CaN during pathogen infection has not been thoroughly elucidated.…”

Section: Introductionmentioning

confidence: 99%

Altering of host larval (Spodoptera exigua) calcineurin activity in response to ascovirus infection

et al. 2019

Pest Management Science

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BACKGROUND Calcineurin (CaN) is involved in numerous cellular processes and Ca2+‐dependent signal transduction pathways. According to our previous transcriptome studies, thousands of host larval (Spodoptera exigua) transcripts were downregulated after the infection of Heliothis virescent ascovirus 3h (HvAV‐3h), while the Spodoptera exigua calcineurin genes (SeCaNs) were significantly upregulated. To understand the regulation of SeCaNs in S. exigua larvae during the infection of HvAV‐3h, the functions of CaN subunit A (SeCaN‐SubA) and CaN binding protein (SeCaN‐BP) were analysed. RESULTS The in vitro assays indicated that the bacterial expressed SeCaN‐SubA is an acid phosphatase, but no phosphatase activity was detected with the purified SeCaN‐BP. The transcription level of SeCaN‐SubA was upregulated after HvAV‐3h infection and the CaN activity was significantly increased after HvAV‐3h infection in S. exigua larvae. Interestingly, the SeCaN‐BP transcripts were only detectable in the HvAV‐3h infected larvae. Further immunoblotting results consistently agree with those obtained by qPCR, indicating that the infection of HvAV‐3h causes the upregulated expression of SeCaN‐SubA and the appearance of SeCaN‐BP. An interaction between the cleaved SeCaN‐SubA and SeCaN‐BP was detected by co‐immunoprecipitation assays, and the expression of SeCaN‐BP in Spodoptera frugiperda‐9 (Sf9) cells can help to increase the CaN activity of SeCaN‐SubA. Further investigations with CaN inhibitors suggested that HvAV‐3h. Further investigations with CaN inhibitors suggested that the inhibition on host larval CaN activity can also inhibit the viral replication of HvAV‐3h. CONCLUSION The increase in CaN activity caused by HvAV‐3h infection might be due to the upregulation of SeCaN‐SubA and the induced expression of SeCaN‐BP, and increased CaN activity is essential for ascoviral replication. © 2019 Society of Chemical Industry

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Mechanistic aspects of the low-molecular-weight phosphatase activity of calcineurin: a model for phosphotyrosyl-protein phosphatases

Cited by 3 publications

References 108 publications

Mechanism of Fe(III) – Zn(II) Purple Acid Phosphatase Based on Crystal Structures

Mechanism of Fe(III) – Zn(II) Purple Acid Phosphatase Based on Crystal Structures

Fluoride Exposure Induces Inhibition of Sodium-and Potassium-Activated Adenosine Triphosphatase (Na+, K+-ATPase) Enzyme Activity: Molecular Mechanisms and Implications for Public Health

Altering of host larval (Spodoptera exigua) calcineurin activity in response to ascovirus infection

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