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In the process of assay optimization, we discovered that PHPT1 is sensitive to a reducing environment and inhibited by transition-metal ions, with one apparent Cu(II) binding site with IC50 value of 500 +/- 20 muM and two apparent Zn(II) binding sites with IC50 values of 25 +/- 1 and 490 +/- 20 muM
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High PHPT1 expression is associated with cancer.
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H2O2 exposure induces selective oxidation of hPHPT1 at Met95, a residue within the substrate binding region. Molecular dynamics simulations suggest that if Met95 oxidation alters hPHPT1 activity, then it will do so by altering the stability of an intermediate state. Mass spectrometry showed that H2O2-induced oxidation does not impact hPHPT1 function negatively.
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PHPT1 was expressed in the epithelium of proximal tubuli and nuclei of clear-cell renal cell carcinoma tissue samples.
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PHPT1 can dephosphorylate phospholysine in chemically phosphorylated histone H1 and polylysine
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The specific degradation of the PHPT1 splice variant indicates that the quality control and the self-guarding of the cellular system works at two levels, first at the RNA level and proteasome level.
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the histidine phosphatase, protein histidine phosphatase 1, inhibits NDPK-B-activated TRPV5 in inside/out patch experiments.
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Overexpression of PHP by the use of a plasmid vector, pIRES2-AcGFP1-PHP, induced apoptosis in HUVEC
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Significantly higher expression levels of PHPT1 protein were found in lung cancer samples than in normal tissues adjacent to lung cancer.
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these data implicate regulatory roles for PHPT1 in a G protein-sensitive step involved in nutrient-induced insulin secretion
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These results demonstrate for the first time that PHP14 may be functionally important in lung cancer cell migration and the invasion of lung cancer cells, mediated partly through modulation of actin cytoskeleton rearrangement.
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Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle.
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In the present work, we have searched for potential active site residues in the human phosphohistidine phosphatase by point mutations of conserved histidine and arginine residues to alanine.
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Overexpression of PHP results in increased dephosphorylation with concomitant inactivation of ACL, thus finally leading to cell damage.
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PHPT-1 functions to negatively regulate CD4 T cells
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Solution structure and catalytic mechanism of human protein histidine phosphatase 1.
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results suggest that an increased activity of protein histidine phosphatase (PHP) impairs neuron cellular function whereas downregulation of PHP does not
