메뉴 건너뛰기




Volumn 153, Issue 1, 2006, Pages 62-70

Fluctuations in Xenopus oocytes protein phosphorylation levels during two-electrode voltage clamp measurements

Author keywords

Current fluctuations; Ion channels; Phosphorylation; PKA; Protein kinases; Protein phosphatases; TEVC

Indexed keywords

CELL PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; MEMBRANE PROTEIN; POTASSIUM CHANNEL; PROTEIN SERINE THREONINE KINASE;

EID: 33646139875     PISSN: 01650270     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jneumeth.2005.10.005     Document Type: Article
Times cited : (12)

References (42)
  • 2
    • 0035029613 scopus 로고    scopus 로고
    • KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel
    • Bockenhauer D., Zilberberg N., and Goldstein S.A. KCNK2: reversible conversion of a hippocampal potassium leak into a voltage-dependent channel. Nat Neurosci 4 5 (2001) 486-491
    • (2001) Nat Neurosci , vol.4 , Issue.5 , pp. 486-491
    • Bockenhauer, D.1    Zilberberg, N.2    Goldstein, S.A.3
  • 3
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0032522719 scopus 로고    scopus 로고
    • Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4, 5-bisphosphate
    • Dell'Acqua M.L., Faux M.C., Thorburn J., Thorburn A., and Scott J.D. Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4, 5-bisphosphate. EMBO J 17 8 (1998) 2246-2260
    • (1998) EMBO J , vol.17 , Issue.8 , pp. 2246-2260
    • Dell'Acqua, M.L.1    Faux, M.C.2    Thorburn, J.3    Thorburn, A.4    Scott, J.D.5
  • 7
    • 0032588030 scopus 로고    scopus 로고
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors
    • 2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors. Proc Natl Acad Sci USA 96 6 (1999) 3269-3274
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.6 , pp. 3269-3274
    • Derkach, V.1    Barria, A.2    Soderling, T.R.3
  • 9
    • 0035287002 scopus 로고    scopus 로고
    • Potassium leak channels and the KCNK family of two-P-domain subunits
    • Goldstein S.A., Bockenhauer D., O'Kelly I., and Zilberberg N. Potassium leak channels and the KCNK family of two-P-domain subunits. Nat Rev Neurosci 2 3 (2001) 175-184
    • (2001) Nat Rev Neurosci , vol.2 , Issue.3 , pp. 175-184
    • Goldstein, S.A.1    Bockenhauer, D.2    O'Kelly, I.3    Zilberberg, N.4
  • 10
    • 0029804030 scopus 로고    scopus 로고
    • ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae
    • Goldstein S.A., Price L.A., Rosenthal D.N., and Pausch M.H. ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 93 23 (1996) 13256-13261
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.23 , pp. 13256-13261
    • Goldstein, S.A.1    Price, L.A.2    Rosenthal, D.N.3    Pausch, M.H.4
  • 11
    • 0033524434 scopus 로고    scopus 로고
    • Sequence correction for: ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae
    • Goldstein S.A., Price L.A., Rosenthal D.N., and Pausch M.H. Sequence correction for: ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 96 1 (1999) 318
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.1 , pp. 318
    • Goldstein, S.A.1    Price, L.A.2    Rosenthal, D.N.3    Pausch, M.H.4
  • 12
    • 0020964899 scopus 로고
    • Serotonin receptors induced by exogenous messenger RNA in Xenopus oocytes
    • Gundersen C.B., Miledi R., and Parker I. Serotonin receptors induced by exogenous messenger RNA in Xenopus oocytes. Proc R Soc Lond B Biol Sci 219 1214 (1983) 103-109
    • (1983) Proc R Soc Lond B Biol Sci , vol.219 , Issue.1214 , pp. 103-109
    • Gundersen, C.B.1    Miledi, R.2    Parker, I.3
  • 13
    • 0021039274 scopus 로고
    • Voltage-operated channels induced by foreign messenger RNA in Xenopus oocytes
    • Gundersen C.B., Miledi R., and Parker I. Voltage-operated channels induced by foreign messenger RNA in Xenopus oocytes. Proc R Soc Lond B Biol Sci 220 1218 (1983) 131-140
    • (1983) Proc R Soc Lond B Biol Sci , vol.220 , Issue.1218 , pp. 131-140
    • Gundersen, C.B.1    Miledi, R.2    Parker, I.3
  • 14
    • 0015230553 scopus 로고
    • Use of frog eggs and oocytes for the study of messenger RNA and its translation in living cells
    • Gurdon J.B., Lane C.D., Woodland H.R., and Marbaix G. Use of frog eggs and oocytes for the study of messenger RNA and its translation in living cells. Nature 233 5316 (1971) 177-182
    • (1971) Nature , vol.233 , Issue.5316 , pp. 177-182
    • Gurdon, J.B.1    Lane, C.D.2    Woodland, H.R.3    Marbaix, G.4
  • 15
    • 1442299852 scopus 로고    scopus 로고
    • Trichloroethanol enhances the activity of recombinant human TREK-1 and TRAAK channels
    • Harinath S., and Sikdar S.K. Trichloroethanol enhances the activity of recombinant human TREK-1 and TRAAK channels. Neuropharmacology 46 5 (2004) 750-760
    • (2004) Neuropharmacology , vol.46 , Issue.5 , pp. 750-760
    • Harinath, S.1    Sikdar, S.K.2
  • 16
    • 0242536407 scopus 로고    scopus 로고
    • Phosphorylation influences neurosteroid modulation of synaptic GABAA receptors in rat CA1 and dentate gyrus neurones
    • Harney S.C., Frenguelli B.G., and Lambert J.J. Phosphorylation influences neurosteroid modulation of synaptic GABAA receptors in rat CA1 and dentate gyrus neurones. Neuropharmacology 45 6 (2003) 873-883
    • (2003) Neuropharmacology , vol.45 , Issue.6 , pp. 873-883
    • Harney, S.C.1    Frenguelli, B.G.2    Lambert, J.J.3
  • 17
    • 0025851846 scopus 로고
    • Sympathetic regulation of cardiac calcium current is due exclusively to cAMP-dependent phosphorylation
    • Hartzell H.C., Mery P.F., Fischmeister R., and Szabo G. Sympathetic regulation of cardiac calcium current is due exclusively to cAMP-dependent phosphorylation. Nature 351 6327 (1991) 573-576
    • (1991) Nature , vol.351 , Issue.6327 , pp. 573-576
    • Hartzell, H.C.1    Mery, P.F.2    Fischmeister, R.3    Szabo, G.4
  • 19
    • 0026080491 scopus 로고
    • Okadaic acid inhibition of KCl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide
    • Jennings M.L., and Schulz R.K. Okadaic acid inhibition of KCl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide. J Gen Physiol 97 (1991) 799-817
    • (1991) J Gen Physiol , vol.97 , pp. 799-817
    • Jennings, M.L.1    Schulz, R.K.2
  • 20
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee H.K., Barbarosie M., Kameyama K., Bear M.F., and Huganir R.L. Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405 6789 (2000) 955-959
    • (2000) Nature , vol.405 , Issue.6789 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 21
    • 0029026780 scopus 로고
    • Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation
    • Levin G., Keren T., Peretz T., Chikvashvili D., Thornhill W.B., and Lotan I. Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation. J Biol Chem 270 (1995) 14611-14618
    • (1995) J Biol Chem , vol.270 , pp. 14611-14618
    • Levin, G.1    Keren, T.2    Peretz, T.3    Chikvashvili, D.4    Thornhill, W.B.5    Lotan, I.6
  • 23
    • 0028324395 scopus 로고
    • Modulation of ion channels by protein phosphorylation and dephosphorylation
    • Levitan I.B. Modulation of ion channels by protein phosphorylation and dephosphorylation. Annu Rev Physiol 56 (1994) 193-212
    • (1994) Annu Rev Physiol , vol.56 , pp. 193-212
    • Levitan, I.B.1
  • 24
    • 0033578649 scopus 로고    scopus 로고
    • Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel
    • Maingret F., Patel A.J., Lesage F., Lazdunski M., and Honore E. Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel. J Biol Chem 274 38 (1999) 26691-26696
    • (1999) J Biol Chem , vol.274 , Issue.38 , pp. 26691-26696
    • Maingret, F.1    Patel, A.J.2    Lesage, F.3    Lazdunski, M.4    Honore, E.5
  • 26
    • 0021110035 scopus 로고
    • Recording of single gamma-aminobutyrate- and acetylcholine-activated receptor channels translated by exogenous mRNA in Xenopus oocytes
    • Miledi R., Parker I., and Sumikawa K. Recording of single gamma-aminobutyrate- and acetylcholine-activated receptor channels translated by exogenous mRNA in Xenopus oocytes. Proc R Soc Lond B Biol Sci 218 1213 (1983) 481-484
    • (1983) Proc R Soc Lond B Biol Sci , vol.218 , Issue.1213 , pp. 481-484
    • Miledi, R.1    Parker, I.2    Sumikawa, K.3
  • 27
    • 0026079765 scopus 로고
    • Functional modulation of brain sodium channels by protein kinase C phosphorylation
    • Numann R., Catterall W.A., and Scheuer T. Functional modulation of brain sodium channels by protein kinase C phosphorylation. Science 254 5028 (1991) 115-118
    • (1991) Science , vol.254 , Issue.5028 , pp. 115-118
    • Numann, R.1    Catterall, W.A.2    Scheuer, T.3
  • 30
    • 10244256419 scopus 로고    scopus 로고
    • Automated higher-throughput compound screening on ion channel targets based on the Xenopus laevis oocyte expression system
    • Pehl U., Leisgen C., Gampe K., and Guenther E. Automated higher-throughput compound screening on ion channel targets based on the Xenopus laevis oocyte expression system. ASSAY Drug Develop Technol 2 5 (2004) 515-524
    • (2004) ASSAY Drug Develop Technol , vol.2 , Issue.5 , pp. 515-524
    • Pehl, U.1    Leisgen, C.2    Gampe, K.3    Guenther, E.4
  • 32
    • 0020693764 scopus 로고
    • Calcium channel modulation by neurotransmitters, enzymes and drugs
    • Reuter H. Calcium channel modulation by neurotransmitters, enzymes and drugs. Nature 301 5901 (1983) 569-574
    • (1983) Nature , vol.301 , Issue.5901 , pp. 569-574
    • Reuter, H.1
  • 33
    • 3242776084 scopus 로고    scopus 로고
    • Signaling cascades regulating NMDA receptor sensitivity to ethanol
    • Ron D. Signaling cascades regulating NMDA receptor sensitivity to ethanol. Neuroscientist 10 4 (2004) 325-336
    • (2004) Neuroscientist , vol.10 , Issue.4 , pp. 325-336
    • Ron, D.1
  • 35
    • 0029205309 scopus 로고
    • Calcium-dependent protein kinases in learning and memory
    • Soderling T.R. Calcium-dependent protein kinases in learning and memory. Adv Second Messenger Phosphoprotein Res 30 (1995) 175-189
    • (1995) Adv Second Messenger Phosphoprotein Res , vol.30 , pp. 175-189
    • Soderling, T.R.1
  • 36
    • 0002919262 scopus 로고
    • Electrophysiological recordings from Xenopus oocytes
    • Sakmann B., and Neher E. (Eds), Plenum Press, New York
    • Stuhmer W., and Parekh A.B. Electrophysiological recordings from Xenopus oocytes. In: Sakmann B., and Neher E. (Eds). Single Channel Recording. 2nd ed. (1995), Plenum Press, New York 341-356
    • (1995) Single Channel Recording. 2nd ed. , pp. 341-356
    • Stuhmer, W.1    Parekh, A.B.2
  • 37
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken K., and Aandahl E.M. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol Rev 84 1 (2004) 137-167
    • (2004) Physiol Rev , vol.84 , Issue.1 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 38
    • 0025273128 scopus 로고
    • Regulation of cardiac L-type calcium current by phosphorylation and G proteins
    • Trautwein W., and Hescheler J. Regulation of cardiac L-type calcium current by phosphorylation and G proteins. Annu Rev Physiol 52 (1990) 257-274
    • (1990) Annu Rev Physiol , vol.52 , pp. 257-274
    • Trautwein, W.1    Hescheler, J.2
  • 39
    • 1842681997 scopus 로고    scopus 로고
    • Calcium-calmodulin-dependent kinase II modulates Kv4.2 channel expression and upregulates neuronal A-type potassium currents
    • Varga A.W., Yuan L.L., Anderson A.E., Schrader L.A., Wu G.Y., Gatchel J.R., et al. Calcium-calmodulin-dependent kinase II modulates Kv4.2 channel expression and upregulates neuronal A-type potassium currents. J Neurosci 24 14 (2004) 3643-3654
    • (2004) J Neurosci , vol.24 , Issue.14 , pp. 3643-3654
    • Varga, A.W.1    Yuan, L.L.2    Anderson, A.E.3    Schrader, L.A.4    Wu, G.Y.5    Gatchel, J.R.6
  • 40
    • 0142243144 scopus 로고    scopus 로고
    • Conditional protein phosphorylation regulates BK channel activity in rat cerebellar Purkinje neurons
    • Widmer H.A., Rowe I.C., and Shipston M.J. Conditional protein phosphorylation regulates BK channel activity in rat cerebellar Purkinje neurons. J Physiol 552 Pt 2 (2003) 379-391
    • (2003) J Physiol , vol.552 , Issue.PART 2 , pp. 379-391
    • Widmer, H.A.1    Rowe, I.C.2    Shipston, M.J.3
  • 41
    • 0032106760 scopus 로고    scopus 로고
    • Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition
    • Zheng F., Gingrich M.B., Traynelis S.F., and Conn P.J. Tyrosine kinase potentiates NMDA receptor currents by reducing tonic zinc inhibition. Nat Neurosci 1 (1998) 185-191
    • (1998) Nat Neurosci , vol.1 , pp. 185-191
    • Zheng, F.1    Gingrich, M.B.2    Traynelis, S.F.3    Conn, P.J.4
  • 42
    • 0033756177 scopus 로고    scopus 로고
    • Opening and closing of KCNKO potassium leak channels is tightly regulated
    • Zilberberg N., Ilan N., Gonzalez-Colaso R., and Goldstein S.A. Opening and closing of KCNKO potassium leak channels is tightly regulated. J Gen Physiol 116 5 (2000) 721-734
    • (2000) J Gen Physiol , vol.116 , Issue.5 , pp. 721-734
    • Zilberberg, N.1    Ilan, N.2    Gonzalez-Colaso, R.3    Goldstein, S.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.