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Volumn 269, Issue 20, 2002, Pages 5016-5023

Identification and characterization of a mammalian 14-kDa phosphohistidine phosphatase

Author keywords

Dephosphorylation; N phosphorylation; Phosphoamidase; Phosphopeptide; Protein histidine phosphatase

Indexed keywords

EDETIC ACID; MESSENGER RNA; OKADAIC ACID; PHOSPHATASE; PHOSPHOHISTIDINE PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOPROTEIN PHOSPHATASE 2C; PHOSPHOSERINE; PHOSPHOTHREONINE; PHOSPHOTYROSINE; UNCLASSIFIED DRUG;

EID: 0036411843     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03206.x     Document Type: Article
Times cited : (91)

References (35)
  • 1
    • 0000183819 scopus 로고
    • Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation
    • Boyer, P.D., DeLuca, M., Ebner, K.E., Hultquist, D.E. & Peter, J.B. (1962) Identification of phosphohistidine in digests from a probable intermediate of oxidative phosphorylation. J. Biol. Chem. 237, 3306-3308.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3306-3308
    • Boyer, P.D.1    DeLuca, M.2    Ebner, K.E.3    Hultquist, D.E.4    Peter, J.B.5
  • 2
    • 0013773646 scopus 로고
    • The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase
    • Mitchell, R.A., Butler, L.G. & Boyer, P.D. (1964) The association of readily-soluble bound phosphohistidine from mitochondria with succinate thiokinase. Biochem. Biophys. Res. Commun. 16, 545-550.
    • (1964) Biochem. Biophys. Res. Commun. , vol.16 , pp. 545-550
    • Mitchell, R.A.1    Butler, L.G.2    Boyer, P.D.3
  • 3
    • 0028829688 scopus 로고
    • Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: A possible regulator of the mitogen-activated protein kinase cascade
    • Matthews, H.R. (1995) Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: A possible regulator of the mitogen-activated protein kinase cascade. Pharmacol. Ther. 67, 323-350.
    • (1995) Pharmacol. Ther. , vol.67 , pp. 323-350
    • Matthews, H.R.1
  • 4
    • 0026347515 scopus 로고
    • Identification of phospho-histidine in proteins and purification of protein-histidine kinases
    • Wei, Y.F. & Matthews, H.R. (1991) Identification of phospho-histidine in proteins and purification of protein-histidine kinases. Methods Enzymol. 200, 388-414.
    • (1991) Methods Enzymol. , vol.200 , pp. 388-414
    • Wei, Y.F.1    Matthews, H.R.2
  • 7
    • 0027400444 scopus 로고
    • Chemotactic stimulation of aggregation-stage Dictyostelium cells induces rapid changes in energy metabolism, as measured by succinic thiokinase phosphorylation
    • Schwander, W.R.E., Jiménez, B., Schwartz, A., Weijer, C.J., Behrens, M., Mazón, M.J. & Fernández-Renart, M. (1993) Chemotactic stimulation of aggregation-stage Dictyostelium cells induces rapid changes in energy metabolism, as measured by succinic thiokinase phosphorylation. Biochim. Biophys. Acta 1176, 175-182.
    • (1993) Biochim. Biophys. Acta , vol.1176 , pp. 175-182
    • Schwander, W.R.E.1    Jiménez, B.2    Schwartz, A.3    Weijer, C.J.4    Behrens, M.5    Mazón, M.J.6    Fernández-Renart, M.7
  • 8
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Moréra, S., Chiadmi, M., LeBras, G., Lascu, I. & Janin, J. (1995) Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry 34, 11062-11070.
    • (1995) Biochemistry , vol.34 , pp. 11062-11070
    • Moréra, S.1    Chiadmi, M.2    LeBras, G.3    Lascu, I.4    Janin, J.5
  • 9
    • 0032482941 scopus 로고    scopus 로고
    • Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate
    • Gottlin, E.B., Rudolph, A.E., Zhao, Y., Matthews, H.R. & Dixon, J.E. (1998) Catalytic mechanism of the phospholipase D superfamily proceeds via a covalent phosphohistidine intermediate. Proc. Natl Acad. Sci. USA 95, 9202-9207.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9202-9207
    • Gottlin, E.B.1    Rudolph, A.E.2    Zhao, Y.3    Matthews, H.R.4    Dixon, J.E.5
  • 10
    • 0034663975 scopus 로고    scopus 로고
    • Mechanism of the bisphosphatase reaction of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by (1)H-15N NMR spectroscopy
    • Okar, D.A., Live, D.H., Devany, M.H. & Lange, A.J. (2000) Mechanism of the bisphosphatase reaction of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase probed by (1)H-15N NMR spectroscopy. Biochemistry 39, 9754-9762.
    • (2000) Biochemistry , vol.39 , pp. 9754-9762
    • Okar, D.A.1    Live, D.H.2    Devany, M.H.3    Lange, A.J.4
  • 12
    • 0025800420 scopus 로고
    • Purification of a protein histidine kinase from the yeast Saccharomyces cerevisiae. The first member of this class of protein kinases
    • Huang, J., Wei, Y., Kim, Y., Osterberg, L. & Matthews, H.R. (1991) Purification of a protein histidine kinase from the yeast Saccharomyces cerevisiae. The first member of this class of protein kinases. J. Biol. Chem. 266, 9023-9031.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9023-9031
    • Huang, J.1    Wei, Y.2    Kim, Y.3    Osterberg, L.4    Matthews, H.R.5
  • 13
    • 0027279242 scopus 로고
    • Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases
    • Kim, Y., Huang, J., Cohen, P. & Matthews, H.R. (1993) Protein phosphatases 1, 2A, and 2C are protein histidine phosphatases. J. Biol. Chem. 268, 18513-18518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18513-18518
    • Kim, Y.1    Huang, J.2    Cohen, P.3    Matthews, H.R.4
  • 14
    • 0029100083 scopus 로고
    • Removal of phosphate from phosphohistidine in proteins
    • Kim, Y., Pesis, K.H. & Matthews, H.R. (1995) Removal of phosphate from phosphohistidine in proteins. Biochim. Biophys. Acta 1268, 221-228.
    • (1995) Biochim. Biophys. Acta , vol.1268 , pp. 221-228
    • Kim, Y.1    Pesis, K.H.2    Matthews, H.R.3
  • 15
    • 0032817262 scopus 로고    scopus 로고
    • Bovine liver phosphoamidase as a protein histidine/lysine phosphatase
    • Hiraishi, H., Yokoi, F. & Kumon, A. (1999) Bovine liver phosphoamidase as a protein histidine/lysine phosphatase. J. Biochem. 126, 368-374.
    • (1999) J. Biochem. , vol.126 , pp. 368-374
    • Hiraishi, H.1    Yokoi, F.2    Kumon, A.3
  • 16
    • 0036176615 scopus 로고    scopus 로고
    • Phosphorylation and dephosphorylation of histidine residues in proteins
    • Klumpp, S. & Krieglstein, J. (2002) Phosphorylation and dephosphorylation of histidine residues in proteins. Eur. J. Biochem. 269, 1067-1071.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1067-1071
    • Klumpp, S.1    Krieglstein, J.2
  • 19
    • 0034655290 scopus 로고    scopus 로고
    • Alteration of the fibrinogen molecule and its phosphorylation state in myocardial infarction patients undergoing thrombolytic treatment
    • Haglund, Å., Ronquist, G., Frithz, G. & Ek, P. (2000) Alteration of the fibrinogen molecule and its phosphorylation state in myocardial infarction patients undergoing thrombolytic treatment. Thromb. Res. 98, 147-156.
    • (2000) Thromb. Res. , vol.98 , pp. 147-156
    • Haglund A.̊1    Ronquist, G.2    Frithz, G.3    Ek, P.4
  • 21
    • 33947448620 scopus 로고
    • Determination of inorganic phosphate. Modification of isobutyl alcohol procedure
    • Martin, J.B. & Doty, D.M. (1949) Determination of inorganic phosphate. Modification of isobutyl alcohol procedure. Anal. Chem. 21, 965-967.
    • (1949) Anal. Chem. , vol.21 , pp. 965-967
    • Martin, J.B.1    Doty, D.M.2
  • 22
    • 0025211779 scopus 로고
    • Quantitation of protein
    • Stoscheck, C.M. (1990) Quantitation of protein. Methods Enzymol. 182, 50-68.
    • (1990) Methods Enzymol. , vol.182 , pp. 50-68
    • Stoscheck, C.M.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T. & Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0027882514 scopus 로고
    • Methionine as translation start signal: A review of the pathway in Escherichia coli
    • Meinnel, T., Mechulam, Y. & Blanquet, S. (1993) Methionine as translation start signal: A review of the pathway in Escherichia coli. Biochimie 75, 1061-1075.
    • (1993) Biochimie , vol.75 , pp. 1061-1075
    • Meinnel, T.1    Mechulam, Y.2    Blanquet, S.3
  • 29
    • 0029034416 scopus 로고
    • Protein histidine phosphatase activity in rat liver and spinach leaves
    • Matthews, H.R. & MacKintosh, C. (1995) Protein histidine phosphatase activity in rat liver and spinach leaves. FEBS Lett. 364, 51-54.
    • (1995) FEBS Lett. , vol.364 , pp. 51-54
    • Matthews, H.R.1    MacKintosh, C.2
  • 30
    • 0014669437 scopus 로고
    • Intermediary phosphorylation of bovine liver nucleoside diphosphate kinase. Studies with a rapid mixing technique
    • Wålinder, O., Zetterqvist, Ø. & Engström, L. (1969) Intermediary phosphorylation of bovine liver nucleoside diphosphate kinase. Studies with a rapid mixing technique. J. Biol. Chem. 244, 1060-1064.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1060-1064
    • Wålinder, O.1    Zetterqvist, Ø.2    Engström, L.3
  • 31
    • 0032489470 scopus 로고    scopus 로고
    • Substrate specificity of human nucleoside-diphosphate kinase revealed by transient kinetic analysis
    • Schaertl, S., Konrad, M. & Greeves, M.A. (1998) Substrate specificity of human nucleoside-diphosphate kinase revealed by transient kinetic analysis. J. Biol. Chem. 273, 5662-5669.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5662-5669
    • Schaertl, S.1    Konrad, M.2    Greeves, M.A.3
  • 32
    • 0028939439 scopus 로고
    • Molecular characterization of an apical early endosomal glycoprotein from developing rat intestinal epithelial cells
    • Speelman, B.A., Allen, K., Grounds, T.L., Neutra, M.R., Kirschhausen, T. & Wilson, J.M. (1995) Molecular characterization of an apical early endosomal glycoprotein from developing rat intestinal epithelial cells. J. Biol. Chem. 270, 1583-1588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1583-1588
    • Speelman, B.A.1    Allen, K.2    Grounds, T.L.3    Neutra, M.R.4    Kirschhausen, T.5    Wilson, J.M.6
  • 33
    • 0031054410 scopus 로고    scopus 로고
    • Targeting of an intestinal apical endosomal protein to endosomes in nonpolarized cells
    • Wilson, J.M. & Colton, T. (1997) Targeting of an intestinal apical endosomal protein to endosomes in nonpolarized cells. J. Cell Biol. 136, 319-330.
    • (1997) J. Cell Biol. , vol.136 , pp. 319-330
    • Wilson, J.M.1    Colton, T.2
  • 35
    • 0034471239 scopus 로고    scopus 로고
    • 2+-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells
    • 2+-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells. J. Cell Sci. 113, 3931-3938.
    • (2000) J. Cell Sci. , vol.113 , pp. 3931-3938
    • Rescher, U.1    Zobiak, N.2    Gerke, V.3


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