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Volumn 11, Issue 1, 2000, Pages 39-50

Is phosphorylation of the α1 subunit at Ser-16 involved in the control of Na,K-ATPase activity by phorbol ester-activated protein kinase C?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CYTOCHROME P450 ISOENZYME; PHORBOL ESTER DERIVATIVE; PHOSPHOLIPASE A2; PROTEIN KINASE C; SERINE; ARACHIDONIC ACID; ENZYME INHIBITOR; OUABAIN; PHORBOL DIBUTYRATE;

EID: 0033621603     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.39     Document Type: Article
Times cited : (28)

References (44)
  • 1
    • 0028033536 scopus 로고
    • Phosphorylation of the Na,K-ATPaSe α-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation
    • Béguin, P., Beggah, A.T., Chibalin, A.V., Burgener-Kairuz, P., Jaisser, F., Mathews, P.M., Rossier, B.C., Cotecchia, S., and Geering, K. (1994). Phosphorylation of the Na,K-ATPaSe α-subunit by protein kinase A and C in vitro and in intact cells. Identification of a novel motif for PKC-mediated phosphorylation. J. Biol. Chem. 269, 24437-24445.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24437-24445
    • Béguin, P.1    Beggah, A.T.2    Chibalin, A.V.3    Burgener-Kairuz, P.4    Jaisser, F.5    Mathews, P.M.6    Rossier, B.C.7    Cotecchia, S.8    Geering, K.9
  • 2
    • 0030062895 scopus 로고    scopus 로고
    • Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase
    • Béguin, P., Beggah, A.T., Cotecchia, S., and Geering, K. (1996a). Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase. Am. J. Physiol. 270, C131-C137.
    • (1996) Am. J. Physiol. , vol.270
    • Béguin, P.1    Beggah, A.T.2    Cotecchia, S.3    Geering, K.4
  • 3
    • 0029809317 scopus 로고    scopus 로고
    • α1 but not α2 or α3 isoforms of Na,K-ATPase are efficiently phosphorylated in a novel protein kinase C motif
    • Béguin, P., Peitsch, M.C., and Geering, K. (1996b). α1 but not α2 or α3 isoforms of Na,K-ATPase are efficiently phosphorylated in a novel protein kinase C motif. Biochemistry 35, 14098-14108.
    • (1996) Biochemistry , vol.35 , pp. 14098-14108
    • Béguin, P.1    Peitsch, M.C.2    Geering, K.3
  • 5
    • 0030937107 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate down-regulates Na,K-ATPase independent of its protein kinase C site: Decrease in basolateral cell surface area
    • Beron, J., Forster, I., Béguin, P., Geering, K., and Verrey, F. (1997). Phorbol 12-myristate 13-acetate down-regulates Na,K-ATPase independent of its protein kinase C site: decrease in basolateral cell surface area. Mol. Biol. Cell 8, 387-398.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 387-398
    • Beron, J.1    Forster, I.2    Béguin, P.3    Geering, K.4    Verrey, F.5
  • 11
    • 0026566941 scopus 로고
    • Phosphorylation of Na,K-ATPase α-subunits in microsomes and in homogenates of Xenopus oocytes resulting from the stimulation of protein kinase A and protein kinase C
    • Chibalin, A.V., Vasilets, L.A., Hennekes, H., Pralong, D., and Geering, K. (1992). Phosphorylation of Na,K-ATPase α-subunits in microsomes and in homogenates of Xenopus oocytes resulting from the stimulation of protein kinase A and protein kinase C. J. Biol. Chem. 267, 22378-22384.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22378-22384
    • Chibalin, A.V.1    Vasilets, L.A.2    Hennekes, H.3    Pralong, D.4    Geering, K.5
  • 14
    • 0027981732 scopus 로고
    • Insulin enhances sodium sensitivity of Na-K-ATPase in isolated rat proximal convoluted tubule
    • Féraille, E., Carranza, M.L., Rousselot, M., and Favre, H. (1994). Insulin enhances sodium sensitivity of Na-K-ATPase in isolated rat proximal convoluted tubule. Am. J. Physiol. 267, F55-F62.
    • (1994) Am. J. Physiol. , vol.267
    • Féraille, E.1    Carranza, M.L.2    Rousselot, M.3    Favre, H.4
  • 15
    • 0027245489 scopus 로고
    • Mechanism of enhanced Na-K-ATPase activity in cortical collecting duct from rats with nephrotic syndrome
    • Féraille, E., Vogt, B., Rousselot, M., Barlet-Bas, C., Cheval, L., Doucet, A., and Favre, H. (1993). Mechanism of enhanced Na-K-ATPase activity in cortical collecting duct from rats with nephrotic syndrome. J. Clin. Invest. 91, 1295-1300.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1295-1300
    • Féraille, E.1    Vogt, B.2    Rousselot, M.3    Barlet-Bas, C.4    Cheval, L.5    Doucet, A.6    Favre, H.7
  • 16
    • 0028032249 scopus 로고
    • Conformation-dependent phosphorylation of Na,K-ATPase by protein kinase A and protein kinase C
    • Feschenko, M.S., and Sweadner, K.J. (1994). Conformation-dependent phosphorylation of Na,K-ATPase by protein kinase A and protein kinase C. J. Biol. Chem. 269, 30436-30444.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30436-30444
    • Feschenko, M.S.1    Sweadner, K.J.2
  • 17
    • 0029054162 scopus 로고
    • Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C
    • Feschenko, M.S., and Sweadner, K.J. (1995). Structural basis for species-specific differences in the phosphorylation of Na,K-ATPase by protein kinase C. J. Biol. Chem. 270, 14072-14077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14072-14077
    • Feschenko, M.S.1    Sweadner, K.J.2
  • 18
    • 0030798864 scopus 로고    scopus 로고
    • 18 occurs in intact cells but does not result in direct inhibition of ATP hydrolysis
    • 18 occurs in intact cells but does not result in direct inhibition of ATP hydrolysis. J. Biol. Chem. 272, 17726-17733.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17726-17733
    • Feschenko, M.S.1    Sweadner, K.J.2
  • 19
    • 0028341655 scopus 로고
    • +-ATPase and effects of site-directed mutagenesis
    • +-ATPase and effects of site-directed mutagenesis. J. Biol. Chem. 269, 9368-9373.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9368-9373
    • Fisone, G.1
  • 21
    • 0028955867 scopus 로고
    • Biotinylation and assessment of membrane polarity: Caveats and methodological concerns
    • Gottardi, C.J., Dunbar, L.A., and Caplan, M.J. (1995). Biotinylation and assessment of membrane polarity: caveats and methodological concerns. Am. J. Physiol. 268, F285-F295.
    • (1995) Am. J. Physiol. , vol.268
    • Gottardi, C.J.1    Dunbar, L.A.2    Caplan, M.J.3
  • 22
    • 0025851275 scopus 로고
    • Endothelin stimulates Na-K-ATPase activity by a protein kinase C-dependent pathway in rabbit aorta
    • Gupta, S., Ruderman, N.B., Cragoe, E.J., and Sussman, I. (1991). Endothelin stimulates Na-K-ATPase activity by a protein kinase C-dependent pathway in rabbit aorta. Am. J. Physiol. 267, H38-H45.
    • (1991) Am. J. Physiol. , vol.267
    • Gupta, S.1    Ruderman, N.B.2    Cragoe, E.J.3    Sussman, I.4
  • 23
    • 0028279809 scopus 로고
    • Role of phosphorylation in desensitization of acetylcholine receptors expressed in Xenopus oocytes
    • Hoffman, P.W., Ravindran, A., and Hunagir, R.L. (1994). Role of phosphorylation in desensitization of acetylcholine receptors expressed in Xenopus oocytes. J. Neurosci. 14, 4185-4195.
    • (1994) J. Neurosci. , vol.14 , pp. 4185-4195
    • Hoffman, P.W.1    Ravindran, A.2    Hunagir, R.L.3
  • 24
    • 0023268192 scopus 로고
    • Phorbol esters and A23187 regulate Na-K pump activity in pancreatic acinar cells
    • Hootman, S.R., Brown, M.E., and Williams, J.A. (1987). Phorbol esters and A23187 regulate Na-K pump activity in pancreatic acinar cells. Am. J. Physiol. 252, G499-G505.
    • (1987) Am. J. Physiol. , vol.252
    • Hootman, S.R.1    Brown, M.E.2    Williams, J.A.3
  • 25
    • 0027759874 scopus 로고
    • Primary sequence and functional expression of a novel β subunit of the P-ATPase gene family
    • Jaisser, F., Horisberger, J.D., and Rossier, B.C. (1993). Primary sequence and functional expression of a novel β subunit of the P-ATPase gene family. Pflügers Arch. 425, 446-452.
    • (1993) Pflügers Arch. , vol.425 , pp. 446-452
    • Jaisser, F.1    Horisberger, J.D.2    Rossier, B.C.3
  • 29
    • 0025944346 scopus 로고
    • Insulin stimulates both the α1 and the α2 isoforms of the rat adipocyte (Na,K) ATPase
    • McGill, D.L., and Guidotti, G. (1991). Insulin stimulates both the α1 and the α2 isoforms of the rat adipocyte (Na,K) ATPase. J. Biol. Chem. 266, 15824-15831.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15824-15831
    • McGill, D.L.1    Guidotti, G.2
  • 30
    • 0027242124 scopus 로고
    • Heterogeneity of protein kinase C-mediated rapid regulation of Na/K-ATPase in kidney epithelial cells
    • Middleton, J.P., Khan, W.A., Collinsworth, G., Hannun, Y.A., and Medford, R.M. (1993). Heterogeneity of protein kinase C-mediated rapid regulation of Na/K-ATPase in kidney epithelial cells. J. Biol. Chem. 268, 15958-15964.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15958-15964
    • Middleton, J.P.1    Khan, W.A.2    Collinsworth, G.3    Hannun, Y.A.4    Medford, R.M.5
  • 32
    • 0028359984 scopus 로고
    • Constitutive mutant and putative regulatory serine phosphorylation site of mammalian MAP kinase kinase (MEK1)
    • Pages, G., Brunet, A., L'Allemain, G., and Pouyssegur, J. (1994). Constitutive mutant and putative regulatory serine phosphorylation site of mammalian MAP kinase kinase (MEK1). EMBO J. 13, 3003-3010.
    • (1994) EMBO J. , vol.13 , pp. 3003-3010
    • Pages, G.1    Brunet, A.2    L'Allemain, G.3    Pouyssegur, J.4
  • 34
    • 0026717815 scopus 로고
    • Intracellular signaling in the regulation of renal Na-K-ATPase
    • Satoh, T., Cohen, H.T., and Katz, A.I. (1992). Intracellular signaling in the regulation of renal Na-K-ATPase. J. Clin. Invest. 89, 1496-1500.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1496-1500
    • Satoh, T.1    Cohen, H.T.2    Katz, A.I.3
  • 35
    • 0027504676 scopus 로고
    • Different mechanisms of renal Na-K-ATPase regulation by protein kinases in proximal and distal nephron
    • Satoh, T., Cohen, H.T., and Katz, A.I. (1993a). Different mechanisms of renal Na-K-ATPase regulation by protein kinases in proximal and distal nephron. Am. J. Physiol. 265, F399-F405.
    • (1993) Am. J. Physiol. , vol.265
    • Satoh, T.1    Cohen, H.T.2    Katz, A.I.3
  • 36
    • 0027510118 scopus 로고
    • Intracellular signaling in the regulation of renal Na-K-ATPase
    • Satoh, T., Cohen, H.T., and Katz, A.I. (1993b). Intracellular signaling in the regulation of renal Na-K-ATPase. J. Clin. Invest. 91, 409-415.
    • (1993) J. Clin. Invest. , vol.91 , pp. 409-415
    • Satoh, T.1    Cohen, H.T.2    Katz, A.I.3
  • 37
    • 0021813222 scopus 로고
    • Renal cytochrome P-450-related arachidonate metabolite inhibits (Na+-K)ATPase
    • Schwartzman, M., Ferreri, N.R., Carroll, M.A., Songu-Mize, E., and McGiff, J.C. (1985). Renal cytochrome P-450-related arachidonate metabolite inhibits (Na+-K)ATPase. Nature 314, 620-622.
    • (1985) Nature , vol.314 , pp. 620-622
    • Schwartzman, M.1    Ferreri, N.R.2    Carroll, M.A.3    Songu-Mize, E.4    McGiff, J.C.5
  • 38
    • 0025942516 scopus 로고
    • The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C
    • Toullec, D., et al. (1991). The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J. Biol. Chem. 266, 15771-15781.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15771-15781
    • Toullec, D.1
  • 39
    • 0030857165 scopus 로고    scopus 로고
    • +-ATPase from mammalian kidneys and Xenopus oocytes by protein kinases: Characterization of the phosphorylation site for protein kinase C
    • +-ATPase from mammalian kidneys and Xenopus oocytes by protein kinases: characterization of the phosphorylation site for protein kinase C. Cell. Physiol. Biochem. 7, 1-18.
    • (1997) Cell. Physiol. Biochem. , vol.7 , pp. 1-18
    • Vasilets, L.A.1
  • 41
    • 0026678143 scopus 로고
    • +-ATPase
    • +-ATPase. FEBS Lett. 324, 301-307.
    • (1992) FEBS Lett. , vol.324 , pp. 301-307
    • Vilsen, B.1
  • 43
    • 0027465923 scopus 로고
    • The amino-terminal segment of the catalytic subunit of kidney Na,K-ATPase regulates the potassium deocclusion pathway of the reaction cycle
    • Wierzbicki, W., and Blostein, R. (1993). The amino-terminal segment of the catalytic subunit of kidney Na,K-ATPase regulates the potassium deocclusion pathway of the reaction cycle. Proc. Natl. Acad. Sci. USA 90, 70-74.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 70-74
    • Wierzbicki, W.1    Blostein, R.2


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