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Volumn 38, Issue 11, 2006, Pages 1901-1913

The γ subunit of Na+, K+-ATPase: Role on ATPase activity and regulatory phosphorylation by PKA

Author keywords

subunit; Na+, K+ ATPase; Phosphorylation; Pig kidney; PKA

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; CYCLIC AMP DEPENDENT PROTEIN KINASE; HYDROXYLAMINE; PHOSPHATE; PHOSPHOTRANSFERASE; PROTEIN SUBUNIT; ENZYME INHIBITOR; LIPID; OUABAIN;

EID: 33748637756     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.05.002     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 0033585007 scopus 로고    scopus 로고
    • The gamma subunit modulates Na (+) and K (+) affinity of the renal Na, K-ATPase
    • Arystarkhova E., Wetzel R.K., Asinovski N.K., and Sweadner K.J. The gamma subunit modulates Na (+) and K (+) affinity of the renal Na, K-ATPase. J. Biol. Chem. 274 (1999) 33183-33185
    • (1999) J. Biol. Chem. , vol.274 , pp. 33183-33185
    • Arystarkhova, E.1    Wetzel, R.K.2    Asinovski, N.K.3    Sweadner, K.J.4
  • 3
    • 0039438642 scopus 로고    scopus 로고
    • The gamma subunit is a specific component of the Na, K-ATPase and modulates its transport function
    • Béguin P., Wang X., Firsov D., Puoti A., Claeys D., Horisberger J.D., et al. The gamma subunit is a specific component of the Na, K-ATPase and modulates its transport function. Embo J. 16 (1997) 4250-4260
    • (1997) Embo J. , vol.16 , pp. 4250-4260
    • Béguin, P.1    Wang, X.2    Firsov, D.3    Puoti, A.4    Claeys, D.5    Horisberger, J.D.6
  • 5
    • 0027757063 scopus 로고
    • Short-term regulation of renal Na-K-ATPase activity: Physiological relevance and cellular mechanisms
    • Bertorello A.M., and Katz A.I. Short-term regulation of renal Na-K-ATPase activity: Physiological relevance and cellular mechanisms. Am. J. Physiol. 34 (1993) F743-F755
    • (1993) Am. J. Physiol. , vol.34
    • Bertorello, A.M.1    Katz, A.I.2
  • 6
    • 0025097988 scopus 로고
    • Renal medullary circulation: Hormonal control
    • Chou S.Y., Porush J.G., and Faubert P.F. Renal medullary circulation: Hormonal control. Kidney Int. 37 (1990) 1-13
    • (1990) Kidney Int. , vol.37 , pp. 1-13
    • Chou, S.Y.1    Porush, J.G.2    Faubert, P.F.3
  • 7
    • 0029137474 scopus 로고
    • Functional significance of the beta-subunit for heterodimeric P-type ATPases
    • Chow D.C., and Forte J.G. Functional significance of the beta-subunit for heterodimeric P-type ATPases. J. Exp. Biol. 198 (1995) 1-17
    • (1995) J. Exp. Biol. , vol.198 , pp. 1-17
    • Chow, D.C.1    Forte, J.G.2
  • 9
    • 0023631796 scopus 로고
    • The "gamma subunit" of Na, K-ATPase: A small, amphiphilic protein with a unique amino acid sequence
    • Collins J.H., and Leszyk J. The "gamma subunit" of Na, K-ATPase: A small, amphiphilic protein with a unique amino acid sequence. Biochemistry 26 (1987) 8665-8669
    • (1987) Biochemistry , vol.26 , pp. 8665-8669
    • Collins, J.H.1    Leszyk, J.2
  • 10
    • 0025115908 scopus 로고
    • Alteration of sodium, potassium-adenosine triphosphatase activity in rabbit ciliary processes by cyclic adenosine monophosphate-dependent protein kinase
    • Delamere N.A., Socci R.R., and King K.L. Alteration of sodium, potassium-adenosine triphosphatase activity in rabbit ciliary processes by cyclic adenosine monophosphate-dependent protein kinase. Invest. Ophthalmol. Vis. Sci. 31 (1990) 2164-2170
    • (1990) Invest. Ophthalmol. Vis. Sci. , vol.31 , pp. 2164-2170
    • Delamere, N.A.1    Socci, R.R.2    King, K.L.3
  • 11
    • 0028837364 scopus 로고
    • Hormonal regulation of the Na (+)-K (+)-ATPase: Mechanisms underlying rapid and sustained changes in pump activity
    • Ewart H.S., and Klip A. Hormonal regulation of the Na (+)-K (+)-ATPase: Mechanisms underlying rapid and sustained changes in pump activity. Am. J. Physiol. 269 (1995) C295-C311
    • (1995) Am. J. Physiol. , vol.269
    • Ewart, H.S.1    Klip, A.2
  • 13
    • 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. Conformation-dependent phosphorylation of Na, K-ATPase by protein kinase A and protein kinase C. J. Biol. Chem. 269 (1994) 30436-30444
    • (1994) J. Biol. Chem. , vol.269 , pp. 30436-30444
    • Feschenko, M.S.1    Sweadner, K.J.2
  • 16
    • 0033563812 scopus 로고    scopus 로고
    • Stimulation of ouabain binding to Na, K-ATPase in 40% dimethyl sulfoxide by a factor from Na, K-ATPase preparations
    • Fontes C.F.L., Lopes F.E.V., Scofano H.M., Barrabin H., and Nørby J.G. Stimulation of ouabain binding to Na, K-ATPase in 40% dimethyl sulfoxide by a factor from Na, K-ATPase preparations. Arch. Biochem. Biophys. 366 (1999) 215-223
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 215-223
    • Fontes, C.F.L.1    Lopes, F.E.V.2    Scofano, H.M.3    Barrabin, H.4    Nørby, J.G.5
  • 18
    • 0017893008 scopus 로고
    • Characterization of a new photoaffinity derivative of ouabain: Labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase
    • Forbush III B., Kaplan J.H., and Hoffman J.F. Characterization of a new photoaffinity derivative of ouabain: Labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 17 (1978) 3667-3676
    • (1978) Biochemistry , vol.17 , pp. 3667-3676
    • Forbush III, B.1    Kaplan, J.H.2    Hoffman, J.F.3
  • 20
    • 0025817601 scopus 로고
    • The functional role of the beta-subunit in the maturation and intracellular transport of Na, K-ATPase
    • Geering K. The functional role of the beta-subunit in the maturation and intracellular transport of Na, K-ATPase. FEBS Lett. 285 (1991) 189-193
    • (1991) FEBS Lett. , vol.285 , pp. 189-193
    • Geering, K.1
  • 21
    • 0027404749 scopus 로고
    • Annual review prize lecture. 'All hands to the sodium pump'
    • Glynn I.M. Annual review prize lecture. 'All hands to the sodium pump'. J. Physiol. 462 (1993) 1-30
    • (1993) J. Physiol. , vol.462 , pp. 1-30
    • Glynn, I.M.1
  • 22
    • 0019887966 scopus 로고
    • The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase
    • Grubmeyer C., and Penefsky H.S. The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 256 (1981) 3718-3727
    • (1981) J. Biol. Chem. , vol.256 , pp. 3718-3727
    • Grubmeyer, C.1    Penefsky, H.S.2
  • 23
    • 0019882825 scopus 로고
    • A proteolipid associated with Na, K-ATPase is not essential for ATPase activity
    • Hardwicke P.M., and Freytag J.W. A proteolipid associated with Na, K-ATPase is not essential for ATPase activity. Biochem. Biophys. Res. Commun. 102 (1981) 250-257
    • (1981) Biochem. Biophys. Res. Commun. , vol.102 , pp. 250-257
    • Hardwicke, P.M.1    Freytag, J.W.2
  • 24
    • 0032515054 scopus 로고    scopus 로고
    • Role of beta-subunit domains in the assembly, stable expression, intracellular routing, and functional properties of Na, K-ATPase
    • Hasler U., Wang X., Crambert G., Beguin P., Jaisser F., Horisberger J.D., et al. Role of beta-subunit domains in the assembly, stable expression, intracellular routing, and functional properties of Na, K-ATPase. J. Biol. Chem. 273 (1998) 30826-30835
    • (1998) J. Biol. Chem. , vol.273 , pp. 30826-30835
    • Hasler, U.1    Wang, X.2    Crambert, G.3    Beguin, P.4    Jaisser, F.5    Horisberger, J.D.6
  • 25
    • 3042672900 scopus 로고    scopus 로고
    • +-ATPase in proximal tubules in young spontaneously hypertensive rats
    • +-ATPase in proximal tubules in young spontaneously hypertensive rats. Hypertension 44 (2004) 95-100
    • (2004) Hypertension , vol.44 , pp. 95-100
    • Hinojos, C.A.1    Doris, P.A.2
  • 27
    • 0014788501 scopus 로고
    • A study of the phosphorylated intermediate of sarcoplasmic reticulum ATPase
    • Inesi G., Maring E., Murphy A., and McFarland B.H. A study of the phosphorylated intermediate of sarcoplasmic reticulum ATPase. Arch. Biochem. Biophys. 138 (1970) 285-294
    • (1970) Arch. Biochem. Biophys. , vol.138 , pp. 285-294
    • Inesi, G.1    Maring, E.2    Murphy, A.3    McFarland, B.H.4
  • 28
    • 0021210752 scopus 로고
    • Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour
    • Jensen J., Nørby J.G., and Ottolenghi P. Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide-binding behaviour. J. Physiol. (Lond.) 346 (1984) 219-241
    • (1984) J. Physiol. (Lond.) , vol.346 , pp. 219-241
    • Jensen, J.1    Nørby, J.G.2    Ottolenghi, P.3
  • 29
    • 0016184723 scopus 로고
    • +)-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate
    • +)-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate. Biochim. Biophys. Acta 356 (1974) 36-52
    • (1974) Biochim. Biophys. Acta , vol.356 , pp. 36-52
    • Jørgensen, P.L.1
  • 30
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na, K-ATPase
    • Kaplan J.H. Biochemistry of Na, K-ATPase. Annu. Rev. Biochem. 71 (2002) 511-535
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 32
    • 0033711925 scopus 로고    scopus 로고
    • Regulation of Na (+)-K (+)-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein
    • Kurihara K., Nakanishi N., and Ueha T. Regulation of Na (+)-K (+)-ATPase by cAMP-dependent protein kinase anchored on membrane via its anchoring protein. Am. J. Physiol. Cell. Physiol. 279 (2000) C1516-C1527
    • (2000) Am. J. Physiol. Cell. Physiol. , vol.279
    • Kurihara, K.1    Nakanishi, N.2    Ueha, T.3
  • 33
    • 0034674066 scopus 로고    scopus 로고
    • A new variant of the gamma subunit of renal Na, K-ATPase. Identification by mass spectrometry, antibody binding and expression in cultured cells
    • Kuster B., Shainskaya A., Pu H.X., Goldshleger R., Blostein R., Mann M., et al. A new variant of the gamma subunit of renal Na, K-ATPase. Identification by mass spectrometry, antibody binding and expression in cultured cells. J. Biol. Chem. 275 (2000) 18441-18446
    • (2000) J. Biol. Chem. , vol.275 , pp. 18441-18446
    • Kuster, B.1    Shainskaya, A.2    Pu, H.X.3    Goldshleger, R.4    Blostein, R.5    Mann, M.6
  • 34
    • 0000203898 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277 (1970) 685-688
    • (1970) Nature , vol.277 , pp. 685-688
    • Laemmli, U.K.1
  • 37
    • 0036213233 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation of purified Na, K-ATPase: C-terminal phosphorylation sites at the alpha- and gamma-subunits close to the inner face of the plasma membrane
    • Mahmmoud Y.A., and Cornelius F. Protein kinase C phosphorylation of purified Na, K-ATPase: C-terminal phosphorylation sites at the alpha- and gamma-subunits close to the inner face of the plasma membrane. Biophys. J. 82 (2002) 1907-1919
    • (2002) Biophys. J. , vol.82 , pp. 1907-1919
    • Mahmmoud, Y.A.1    Cornelius, F.2
  • 38
    • 0141844566 scopus 로고    scopus 로고
    • Regulation of Na, K-ATPase by PLMS, the phospholemman-like protein from shark: Molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS
    • Mahmmoud Y.A., Cramb G., Maunsbach A.B., Cutler C.P., Meischke L., and Cornelius F. Regulation of Na, K-ATPase by PLMS, the phospholemman-like protein from shark: Molecular cloning, sequence, expression, cellular distribution, and functional effects of PLMS. J. Biol. Chem. 278 (2003) 37427-37438
    • (2003) J. Biol. Chem. , vol.278 , pp. 37427-37438
    • Mahmmoud, Y.A.1    Cramb, G.2    Maunsbach, A.B.3    Cutler, C.P.4    Meischke, L.5    Cornelius, F.6
  • 39
    • 0034680861 scopus 로고    scopus 로고
    • Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na, K-ATPase by protein kinase C via a novel member of the FXYDY family
    • Mahmmoud Y.A., Vorum H., and Cornelius F. Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na, K-ATPase by protein kinase C via a novel member of the FXYDY family. J. Biol. Chem. 275 (2000) 35969-35977
    • (2000) J. Biol. Chem. , vol.275 , pp. 35969-35977
    • Mahmmoud, Y.A.1    Vorum, H.2    Cornelius, F.3
  • 40
    • 0002429588 scopus 로고
    • Preparation of [alpha-32p] and [gamma-32p] nucleoside triphosphate with high specific activity
    • Morel C.M. (Ed). Rio de Janeiro, Fiocruz
    • Maia J.C.C., Gomes S.L., and Juliani M.H. Preparation of [alpha-32p] and [gamma-32p] nucleoside triphosphate with high specific activity. In: Morel C.M. (Ed). Genes and antigenes of parasites-A laboratory manual proceedings. Rio de Janeiro, Fiocruz (1983) 145-157
    • (1983) Genes and antigenes of parasites-A laboratory manual proceedings , pp. 145-157
    • Maia, J.C.C.1    Gomes, S.L.2    Juliani, M.H.3
  • 41
    • 0027162078 scopus 로고
    • Structure of the Na, K-ATPase
    • Mercer R.W. Structure of the Na, K-ATPase. Int. Rev. Cytol. 137 (1993) 139-168
    • (1993) Int. Rev. Cytol. , vol.137 , pp. 139-168
    • Mercer, R.W.1
  • 42
    • 0027281005 scopus 로고
    • Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na, K-ATPase
    • Mercer R.W., Biemensderfer D., Bliss Jr. D.P., Collins J.H., and Forbush III B. Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na, K-ATPase. J. Cell Biol. 121 (1993) 579-586
    • (1993) J. Cell Biol. , vol.121 , pp. 579-586
    • Mercer, R.W.1    Biemensderfer, D.2    Bliss Jr., D.P.3    Collins, J.H.4    Forbush III, B.5
  • 43
    • 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. Heterogeneity of protein kinase C-mediated rapid regulation of Na/K-ATPase in kidney epithelial cells. J. Biol. Chem. 268 (1993) 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
  • 44
    • 0031057630 scopus 로고    scopus 로고
    • Short-term vs. sustained inhibition of proximal tubule Na, K-ATPase activity by dopamine: Cellular mechanisms
    • Pinto-Do-O P.C., Chibalin A.V., Katz A.I., Da Silva P.S., and Bertorello A.M. Short-term vs. sustained inhibition of proximal tubule Na, K-ATPase activity by dopamine: Cellular mechanisms. Clin. Exp. Hypertens. 19 (1997) 73-86
    • (1997) Clin. Exp. Hypertens. , vol.19 , pp. 73-86
    • Pinto-Do-O, P.C.1    Chibalin, A.V.2    Katz, A.I.3    Da Silva, P.S.4    Bertorello, A.M.5
  • 45
    • 0035827529 scopus 로고    scopus 로고
    • Functional role and immunocytochemical localization of the gamma a and gamma b forms of the Na, K-ATPase gamma subunit
    • Pu H.X., Cluzeaud F., Goldshlegger R., Karlish S.J.D., Farman N., and Blostein R. Functional role and immunocytochemical localization of the gamma a and gamma b forms of the Na, K-ATPase gamma subunit. J. Biol. Chem. 276 (2001) 20370-20378
    • (2001) J. Biol. Chem. , vol.276 , pp. 20370-20378
    • Pu, H.X.1    Cluzeaud, F.2    Goldshlegger, R.3    Karlish, S.J.D.4    Farman, N.5    Blostein, R.6
  • 46
  • 48
    • 0036385728 scopus 로고    scopus 로고
    • Oligomerization of a peptide derived from the transmembrane region of the sodium pump gamma subunit: Effect of the pathological mutation G41R
    • Therien A.G., and Deber C.M. Oligomerization of a peptide derived from the transmembrane region of the sodium pump gamma subunit: Effect of the pathological mutation G41R. J. Mol. Biol. 322 (2002) 583-590
    • (2002) J. Mol. Biol. , vol.322 , pp. 583-590
    • Therien, A.G.1    Deber, C.M.2
  • 49
    • 0031434245 scopus 로고    scopus 로고
    • Tissue-specific distribution and modulatory role of the gamma subunit of the Na, K-ATPase
    • Therien A.G., Goldshleger R., Karlish S.J.D., and Blostein R. Tissue-specific distribution and modulatory role of the gamma subunit of the Na, K-ATPase. J. Biol. Chem. 272 (1997) 32628-32634
    • (1997) J. Biol. Chem. , vol.272 , pp. 32628-32634
    • Therien, A.G.1    Goldshleger, R.2    Karlish, S.J.D.3    Blostein, R.4
  • 50
    • 0033617311 scopus 로고    scopus 로고
    • Expression and functional role of the gamma subunit of the Na, K-ATPase in mammalian cells
    • Therien A.G., Karlish S.J.D., and Blostein R. Expression and functional role of the gamma subunit of the Na, K-ATPase in mammalian cells. J. Biol. Chem. 274 (1999) 12252-12256
    • (1999) J. Biol. Chem. , vol.274 , pp. 12252-12256
    • Therien, A.G.1    Karlish, S.J.D.2    Blostein, R.3
  • 51
    • 0036509461 scopus 로고    scopus 로고
    • Dimethyl sulfoxide-induced conformational state of Na(+)/K(+)-ATPase studied by proteolytic cleavage
    • Tribuzy A.V.B., Fontes C.F.L., Nørby J.G., and Barrabin H. Dimethyl sulfoxide-induced conformational state of Na(+)/K(+)-ATPase studied by proteolytic cleavage. Arch. Biochem. Biophys. 399 (2002) 89-95
    • (2002) Arch. Biochem. Biophys. , vol.399 , pp. 89-95
    • Tribuzy, A.V.B.1    Fontes, C.F.L.2    Nørby, J.G.3    Barrabin, H.4
  • 53
    • 4744368156 scopus 로고    scopus 로고
    • Stress-induced expression of the gamma subunit (FXYD2) modulates Na, K-ATPase activity and cell growth
    • Wetzel R.K., Pascoa J.L., and Arystarkhova E. Stress-induced expression of the gamma subunit (FXYD2) modulates Na, K-ATPase activity and cell growth. J. Biol. Chem. 279 (2004) 41750-41757
    • (2004) J. Biol. Chem. , vol.279 , pp. 41750-41757
    • Wetzel, R.K.1    Pascoa, J.L.2    Arystarkhova, E.3
  • 54
    • 0142135344 scopus 로고    scopus 로고
    • Modulation of Na, K-ATPase by the gamma subunit: Studies with transfected cells and transmembrane mimetic peptides
    • Zouzoulas A., Therien A.G., Scanzano R., Deber C., and Blostein R. Modulation of Na, K-ATPase by the gamma subunit: Studies with transfected cells and transmembrane mimetic peptides. J. Biol. Chem. 278 (2003) 40437-40441
    • (2003) J. Biol. Chem. , vol.278 , pp. 40437-40441
    • Zouzoulas, A.1    Therien, A.G.2    Scanzano, R.3    Deber, C.4    Blostein, R.5


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