메뉴 건너뛰기




Volumn 6, Issue 3, 1996, Pages 318-323

Regulation of potassium channels by protein kinases

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; POTASSIUM CHANNEL; PROTEIN KINASE; PROTEIN SERINE KINASE; TYROSINE;

EID: 0030176232     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(96)80114-0     Document Type: Article
Times cited : (168)

References (45)
  • 2
    • 0026341651 scopus 로고
    • A phosphorylatlon site in the Na+ channel required for modulation by protein klnase C
    • Wesl JW, Numann R, Murphy BJ, Scheuer T, Catterall WAA phosphorylatlon site In the Na+ channel required for modulation by protein klnase C. Science 1991, 294:866-868.
    • (1991) Science , vol.294 , pp. 866-868
    • Wesl, J.W.1    Numann, R.2    Murphy, B.J.3    Scheuer, T.4    Catterall, W.A.5
  • 3
    • 0027496454 scopus 로고
    • Convergent regulation of sodium channels by protein klnase C and cAMP-dependent protein klnase
    • Li M, Wast JW, Numann R, Murphy BJ, Scheuer T, Catterall WAConvergent regulation of sodium channels by protein klnase C and cAMP-dependent protein klnase. Science 1993, 261:1439-1442
    • (1993) Science , vol.261 , pp. 1439-1442
    • Li, M.1    Wast, J.W.2    Numann, R.3    Murphy, B.J.4    Scheuer, T.5    Catterall, W.A.6
  • 4
    • 0028127059 scopus 로고
    • 2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein klnase
    • Voltage-dependent potentiation of L-type calcium currents requires phosphorylation of the calcium channel by PKA. This potenttation can be blocked by a peptide derived from a PKA-anchoring protein, suggesting that close physical proximity of the channel with the kinase is required for channel modulation
    • 2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein klnase. Proc Natl Acad Sci USA 1994, 91:11492-11496. Voltage-dependent potentiation of L-type calcium currents requires phosphorylation of the calcium channel by PKA. This potenttation can be blocked by a peptide derived from a PKA-anchoring protein, suggesting that close physical proximity of the channel with the kinase is required for channel modulation.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11492-11496
    • Johnson, B.O.1    Scheuer, T.2    Catterall, W.A.3
  • 5
    • 0028212976 scopus 로고
    • Regulation of the cloned L-type cardiac calcium channel by cycllc-AMPdependent protein kinase
    • Perez-Reyes E, Yuan W, Wei X, Bers DMRegulation of the cloned L-type cardiac calcium channel by cycllc-AMPdependent protein kinase. FEBS Lett 1994, 342:119-123.
    • (1994) FEBS Lett , vol.342 , pp. 119-123
    • Perez-Reyes, E.1    Yuan, W.2    Wei, X.3    Bers, D.M.4
  • 6
    • 0029041248 scopus 로고
    • Phosphorylatlon of preayneptle and postsynaptlc calcium channels by cAMP-dependent protein kinase in hippocampal neurons
    • Hell JW, Yokoyama CT, Breeze U, Chavkin C, Catterall WAPhosphorylatlon of preayneptle and postsynaptlc calcium channels by cAMP-dependent protein kinase In hippocampal neurons. EM BO J 1995, 14:3036-3044.
    • (1995) EM BO J , vol.14 , pp. 3036-3044
    • Hell, J.W.1    Yokoyama, C.T.2    Breeze, U.3    Chavkin, C.4    Catterall, W.A.5
  • 7
    • 0028238794 scopus 로고
    • Insulin-Ilk growth factor-1 induces a rapid Increase in calcium currents and spontaneous membrane activity in clonal pituitary cells
    • Selinfreund RH, Blair LACInsulin-Ilk growth factor-1 induces a rapid Increase in calcium currents and spontaneous membrane activity in clonal pituitary cells. Moi Pharmacol 1994, 45:1215-1220.
    • (1994) Moi Pharmacol , vol.45 , pp. 1215-1220
    • Selinfreund, R.H.1    Blair, L.A.C.2
  • 8
    • 0026611044 scopus 로고
    • 2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites in isolated Aptysin neurons
    • 2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites In isolated Aptysin neurons. Neuron 1992, 8:863-889.
    • (1992) Neuron , vol.8 , pp. 863-889
    • Knox, R.J.1    Quattrocki, E.A.2    Connor, J.A.3
  • 9
    • 0029960047 scopus 로고    scopus 로고
    • Insulin receptor in Aplysio neurons: Characterization, molecular cloning and modulation on ion currents
    • Demonstration that an endogenous receptor tyrosine kinase in an Aplysia neuron acutely regulates potassium and calcium channels
    • Jonas EA, Knox RJ, Kaczmarek LK. Schwaru JH. Solomon DH: Insulin receptor In Aplysio neurons: characterization, molecular cloning and modulation on ion currents. J Neurosci 1996, 16:1645-1658. Demonstration that an endogenous receptor tyrosine kinase in an Aplysia neuron acutely regulates potassium and calcium channels.
    • (1996) J Neurosci , vol.16 , pp. 1645-1658
    • Jonas, E.A.1    Knox, R.J.2    Kaczmarek, L.K.3    Schwaru, J.H.4    Solomon, D.H.5
  • 10
    • 0002375421 scopus 로고
    • Voltage-gated potassium channel genes
    • Boca Raton, Florida: CRC Press; A comprehensive review covering studies up to 1995 of the Shaker superfamily of channels
    • Chandy KG, Gutman GAVoltage-gated potassium channel genes. In CRC Handbook of Receptors and Channels. Boca Raton, Florida: CRC Press; 1995:1-71. A comprehensive review covering studies up to 1995 of the Shaker superfamily of channels.
    • (1995) CRC Handbook of Receptors and Channels , pp. 1-71
    • Chandy, K.G.1    Gutman, G.A.2
  • 11
    • 0029019252 scopus 로고
    • New potassium gene families in flies and mammals: From mutants to molecules
    • Ganetzky B, Warmke JW, Robertson G, Pallanck LNew potassium gene families in flies and mammals: from mutants to molecules. Soc Gen Physiol Ser 1995, 50:29-39.
    • (1995) Soc Gen Physiol Ser , vol.50 , pp. 29-39
    • Ganetzky, B.1    Warmke, J.W.2    Robertson, G.3    Pallanck, L.4
  • 12
    • 0029099458 scopus 로고
    • Kaczmarek LK, Goidstein SAN: A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
    • Ketchum KA, Joiner WJ, Sellers AJ. Kaczmarek LK, Goidstein SAN: A new family of outwardly rectifying potassium channel proteins with two pore domains In tandem. Nature 1995, 376:690-695
    • (1995) Nature , vol.376 , pp. 690-695
    • Ketchum, K.A.1    Joiner, W.J.2    Sellers, A.J.3
  • 13
    • 85081184909 scopus 로고    scopus 로고
    • Properties and regulation of the m in K potassium channel
    • in press
    • Kaczmarek LKProperties and regulation of the m in K potassium channel. Physiol Rev 1996, in press.
    • (1996) Physiol Rev
    • Kaczmarek, L.K.1
  • 15
    • 0028949194 scopus 로고
    • Molecular cloning and functional expression of a novel potassium channel β-subunit from human atrium
    • Majumder K, Biasi MD, Wang Z, Wible BAMolecular cloning and functional expression of a novel potassium channel β-subunit from human atrium. FEBS Lett 1995, 361:13-16.
    • (1995) FEBS Lett , vol.361 , pp. 13-16
    • Majumder, K.1    Biasi, M.D.2    Wang, Z.3    Wible, B.A.4
  • 16
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi T, Zagotta WN, Aldrich RWBiophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 1990, 250:533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 17
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by peptide derived from ShB
    • Zagotta WN, Hoshi T, Aldrich RWRestoration of inactivation in mutants of Shaker potassium channels by peptide derived from ShB. Science 1990, 250:568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 18
    • 0028136017 scopus 로고
    • State-dependent Inactivation ol the Kv3 potassium channel
    • Marom S, Levitan IBState-dependent Inactivation ol the Kv3 potassium channel. Biophys J 1994, 67:579-589.
    • (1994) Biophys J , vol.67 , pp. 579-589
    • Marom, S.1    Levitan, I.B.2
  • 19
    • 0028605349 scopus 로고
    • Elimination of rapid potassium channel inactivation by phosphorylation of the Inactivation gate
    • A dramatic example of how phosphorylation of sites on the ammo terminus of Ihe Kv3.4 channel converts it from a rapidly inactivating 'A-type' channel into a 'delayed rectifier' channel
    • Covarrubias M, Wei A, Salkott L, Vyas TBElimination of rapid potassium channel inactivation by phosphorylation of the Inactivation gate. Neuron 1994,13:1403-1412. A dramatic example of how phosphorylation of sites on the ammo terminus of Ihe Kv3.4 channel converts it from a rapidly inactivating 'A-type' channel into a 'delayed rectifier' channel.
    • (1994) Neuron , vol.13 , pp. 1403-1412
    • Covarrubias, M.1    Wei, A.2    Salkott, L.3    Vyas, T.B.4
  • 20
    • 0026525699 scopus 로고
    • Modulation by CAMP of a slowly activating potassium channel expressed in Xenopus oocytes
    • Blumenthal EM, Kaczmarek LKModulation by CAMP of a slowly activating potassium channel expressed in Xenopus oocytes. J A/ewosc/ 1992,12:290-296,
    • (1992) J A/ewosc , vol.12 , pp. 290-296
    • Blumenthal, E.M.1    Kaczmarek, L.K.2
  • 21
    • 0029026780 scopus 로고
    • Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation
    • An examination of the role of channel phosphorylation in the response of oocytes expressing Kvl.1 to prolonged treatment (10-16h) with a cyclic AMP analog. This work contrasts with most other studies, which have examined only acute effects of cyclic AMP
    • Levin G, Keren T, Peretz T, Chikvashvili D, Thornhill WB: Regulation of RCK1 currents with a cAMP analog via enhanced protein synthesis and direct channel phosphorylation. J Biol Chem 1995, 270:14611-14618. An examination of the role of channel phosphorylation in the response of oocytes expressing Kvl.1 to prolonged treatment (10-16h) with a cyclic AMP analog. This work contrasts with most other studies, which have examined only acute effects of cyclic AMP.
    • (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
  • 22
    • 0028321838 scopus 로고
    • + channel inactivation gating by the cAMP-dependent protein kinase
    • A study of the aclion of alkaline phosphalase on N-type inactivation in normal and mutant Shaker channels
    • + channel inactivation gating by the cAMP-dependent protein kinase. Neuron 1994, 12:1097-1109. A study of the aclion of alkaline phosphalase on N-type inactivation in normal and mutant Shaker channels.
    • (1994) Neuron , vol.12 , pp. 1097-1109
    • Drain, P.1    Dubin, A.E.2    Aldrich, R.W.3
  • 23
    • 0029016295 scopus 로고
    • Intracellular and extracellular amlno acids that influence C-type inactivation and its modulation in a voltage-dependent potassium channel
    • The rate of C-type inactivation of the Kv1.3 channel was found to be markedly stowed by simultaneous mutation of three putative phosphorylation sites
    • Kupper J, Bowlby MR, Marom S, Levitan IBIntracellular and extracellular amlno acids that influence C-type inactivation and its modulation in a voltage-dependent potassium channel. Pflugers Arch 1995, 430:1 -11. The rate of C-type inactivation of the Kv1.3 channel was found to be markedly stowed by simultaneous mutation of three putative phosphorylation sites.
    • (1995) Pflugers Arch , vol.430 , pp. 1-11
    • Kupper, J.1    Bowlby, M.R.2    Marom, S.3    Levitan, I.B.4
  • 25
    • 0028365184 scopus 로고
    • Cyclic AMP modulates fast axonal transport in Aplysia bag call neurons by Increasing the probability of single organelle movement
    • Azhderian EM, Hefner D, Lin C-H, Kaczmarek LK, Forscher P: Cyclic AMP modulates fast axonal transport In Aplysia bag call neurons by Increasing the probability of single organelle movement Neuron 1994,12:1223-1233.
    • (1994) Neuron , vol.12 , pp. 1223-1233
    • Azhderian, E.M.1    Hefner, D.2    Lin, C.-H.3    Kaczmarek, L.K.4    Forscher, P.5
  • 27
    • 0028008620 scopus 로고
    • Molecular basis of cardiac potassium channel stimulation by protein kinase a
    • A demonstration that the amplitude of current carried by Kv1.2 channel is enhanced by PKA, an effect that required a PKA site on the amino terminus
    • Huang X-Y, Morielli AD, Peralta EGMolecular basis of cardiac potassium channel stimulation by protein kinase A. Proc Natl Acad Sci USA 1994, 91:824-62B. A demonstration that the amplitude of current carried by Kv1.2 channel is enhanced by PKA, an effect that required a PKA site on the amino terminus.
    • (1994) Proc Natl Acad Sci USA , vol.91
    • Huang, X.-Y.1    Morielli, A.D.2    Peralta, E.G.3
  • 28
    • 0028024075 scopus 로고
    • Modulation by protein kinase a of a cloned rat brain potassium channel expressed in Xenopus oocytes
    • Wilson GG, O'Neill CA, Sivaprasadarao A, Findlay JBC, Wray DModulation by protein kinase A of a cloned rat brain potassium channel expressed in Xenopus oocytes. Pflugers Arch 1994, 428:186-193
    • (1994) Pflugers Arch , vol.428 , pp. 186-193
    • Wilson, G.G.1    O'Neill, C.A.2    Sivaprasadarao, A.3    Jbc, F.4    Wray, D.5
  • 29
    • 0029166678 scopus 로고
    • Phosphorylation of the nlcotlnlc acetylcholine receptor by protein tyroslne klnases
    • Swope SL, Ou 2, Huganir RLPhosphorylation of the nlcotlnlc acetylcholine receptor by protein tyroslne klnases. Ann NY Acad Sci 1995, 757:197-214.
    • (1995) Ann NY Acad Sci , vol.757 , pp. 197-214
    • Swope, S.L.1    Huganir, R.L.2
  • 30
    • 0027715423 scopus 로고
    • Mode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyroslne phosphatase
    • Wilson GF, Kaczmarek LKMode-switching of a voltage-gated cation channel is mediated by a protein kinase A-regulated tyroslne phosphatase. Nature 1993, 366:433-430
    • (1993) Nature , vol.366 , pp. 433-1430
    • Wilson, G.F.1    Kaczmarek, L.K.2
  • 31
    • 0024369312 scopus 로고
    • Régulation of ionic currents in pheochromocytoma cells by nerve growth factor and dexamethasone
    • Garber SS, Hoshi T, Aldrich RWRégulation of ionic currents in pheochromocytoma cells by nerve growth factor and dexamethasone. J Neurosci 1969, 9:3976-3987.
    • (1969) J Neurosci , vol.9 , pp. 3976-3987
    • Garber, S.S.1    Hoshi, T.2    Aldrich, R.W.3
  • 33
    • 0028256231 scopus 로고
    • Modulation of a voltage-activated potassium channel by peptide growth factor receptors
    • Timpe LC, Fantl WJModulation of a voltage-activated potassium channel by peptide growth factor receptors. J Neurosel 1994, 14:1195-1201.
    • (1994) J Neurosel , vol.14 , pp. 1195-1201
    • Timpe, L.C.1    Fantl, W.J.2
  • 34
    • 0027146670 scopus 로고
    • Tyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled ml muscarinic acetylcholine receptor
    • Huang X-Y, Morielli AD, Peralta EGTyrosine kinase-dependent suppression of a potassium channel by the G protein-coupled ml muscarinic acetylcholine receptor. Cell 1993, 75:1145-1156.
    • (1993) Cell , vol.75 , pp. 1145-1156
    • Huang, X.-Y.1    Morielli, A.D.2    Peralta, E.G.3
  • 35
    • 0029916913 scopus 로고    scopus 로고
    • Tyroslne phosphorylation of the Kv1.3 potassium channel
    • A direct demonstration that there is continual phosphorylalion and desphosphorylation of lyrosine residues of the Kvl.3 delayed rectifier potassium channel, and that the state of phosphorylation influences the amplitude of the potassium current
    • Holmes TC, Fadool DA, Levitan IBTyroslne phosphorylation of the Kv1.3 potassium channel. J Neumsci 1996, 16:1581-1590. A direct demonstration that there is continual phosphorylalion and desphosphorylation of lyrosine residues of the Kvl.3 delayed rectifier potassium channel, and that the state of phosphorylation influences the amplitude of the potassium current
    • (1996) J Neumsci , vol.16 , pp. 1581-1590
    • Holmes, T.C.1    Fadool, D.A.2    Levitan, I.B.3
  • 36
    • 0029154733 scopus 로고
    • 2+- Induced regulation of ion channel and MAP kinase functions
    • The authors identify a novel protein tyrosine kinase that directly phosphorylales the Kv1.2 channel. This is the first identification of a tyrosine kinase that directly phosphorylates a potassium channel
    • 2+- induced regulation of ion channel and MAP kinase functions. Nature 1995, 376:737-745. The authors identify a novel protein tyrosine kinase that directly phosphorylales the Kv1.2 channel. This is the first identification of a tyrosine kinase that directly phosphorylates a potassium channel.
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno, H.2    Martinez, R.3    Canoll, P.4    Peles, E.5    Musacchio, J.M.6    Plowman, G.D.7    Rudy, B.8    Schlessinger, J.9
  • 37
    • 0028670803 scopus 로고
    • + channels are regulated Independently protein kineses and ATP hydrolysis
    • The authors show that rundown of the Kir2.1 channel in excised patches can be prevented by ATP. PKA also enhances current amplitude in channels that have been pre-lreated with ATP. An activator of PKC caused a decrease in current
    • + channels are regulated Independently protein kineses and ATP hydrolysis. Neuron 1994, 3:1413-1420 The authors show that rundown of the Kir2.1 channel in excised patches can be prevented by ATP. PKA also enhances current amplitude in channels that have been pre-lreated with ATP. An activator of PKC caused a decrease in current.
    • (1994) Neuron , vol.3 , pp. 1413-1420
    • Fakler, B.1    Brandie, U.2    Glowatzki, E.3    Zenner, H.-P.4    Ruppersberg, J.P.5
  • 38
    • 0028132026 scopus 로고
    • a4 epithelial cell line by calcium, nucleotJdes and kinases
    • Inwardly rectifying potassium currents in a cell line were found to be enhanced by ATP and by PKA, which could prevent rundown of channel activity. Application of PKC to membrane patches inhibited single channel activity
    • a4 epithelial cell line by calcium, nucleotJdes and kinases. J Membr Biol 1994, 142:255-266. Inwardly rectifying potassium currents in a cell line were found to be enhanced by ATP and by PKA, which could prevent rundown of channel activity. Application of PKC to membrane patches inhibited single channel activity.
    • (1994) J Membr Biol , vol.142 , pp. 255-266
    • Tabcharani, J.A.1    Boucher, A.2    Eng, J.W.L.3    Hanrahan, J.W.4
  • 39
    • 0029011163 scopus 로고
    • Protein kinase C-mediated inhibition of an inward rectifier potassium channel by substance P in nucleus basalis neurons
    • The authors provide a clear example of modulation of a G-protein-regulated inward rectifier channel by a neuropeptide. The effects of substance P were mimicked by PKC and were rendered irreversible by the phosphatase inhibitor, okadaic acid
    • Takano K, Stanfield PR, Nakajima S, Nakajima YProtein kinase C-mediated inhibition of an inward rectifier potassium channel by substance P in nucleus basalis neurons. Neuron 1995, 14:999-1008. The authors provide a clear example of modulation of a G-protein-regulated inward rectifier channel by a neuropeptide. The effects of substance P were mimicked by PKC and were rendered irreversible by the phosphatase inhibitor, okadaic acid.
    • (1995) Neuron , vol.14 , pp. 999-1008
    • Takano, K.1    Stanfield, P.R.2    Nakajima, S.3    Nakajima, Y.4
  • 40
    • 0029123601 scopus 로고
    • FAK and associated proteins: Role in neuritogenesis
    • FAK a non-receptor tyrosine kinase. The authors suggest that activation of inward rectifier channels is required for activation of the kinase
    • FAK a non-receptor tyrosine kinase. The authors suggest that activation of inward rectifier channels is required for activation of the kinase.
    • (1995) Biochem Bropbys Res Comm , vol.210 , pp. 823-829
    • Bianehi, L.1    Arcangeli, A.2    Bartolini, P.3    Mugnai, G.4    Wanke, E.5    Olivotto, M.6
  • 41
    • 0028100839 scopus 로고
    • +channel activity involves phosphorylatlon processe
    • The inward rectifier channel ROMK1 was expressed in Xenopus oocytes. Rundown of channel activity was observed in cell-free patches but was prevented by the phosphatase inhibitor vanadate, but not by okadaic acid, suggesting thai the channel is regulated by the serine/threonine phosphalase PP2C or by a tyrosine phosphatase. Channel activity was also found to be enhanced by PKA and inhibited by an inhibitor of PKA
    • +channel activity involves phosphorylatlon processe. Proc Natl Acad Sci USA 1994, 91:8077-8081. The inward rectifier channel ROMK1 was expressed in Xenopus oocytes. Rundown of channel activity was observed in cell-free patches but was prevented by the phosphatase inhibitor vanadate, but not by okadaic acid, suggesting thai the channel is regulated by the serine/threonine phosphalase PP2C or by a tyrosine phosphatase. Channel activity was also found to be enhanced by PKA and inhibited by an inhibitor of PKA.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8077-8081
    • McNicholas, C.M.1    Wang, W.2    Ho, K.3    Hebert, S.C.4    Giebisch, G.5
  • 42
    • 0028822697 scopus 로고
    • Role of tyrosine phosphorylatlon in potassium channel activation
    • An endogenous calcium-activated potassium conductance in CHO cells was shown to be increased by activation ol a transfected prolactin receptor. This effect was blocked by tyrosine kinaso inhibitors and also by an anti-peptide antibody directed against the JAK2 tyrosine fcinase
    • Prevarskaya NB, Skryma RM, Vacher P, Daniel N, Djiane J, Duly BRole of tyrosine phosphorylatlon In potassium channel activation. J Biol Chem 1995, 270:24292-24299. An endogenous calcium-activated potassium conductance in CHO cells was shown to be increased by activation ol a transfected prolactin receptor. This effect was blocked by tyrosine kinaso inhibitors and also by an anti-peptide antibody directed against the JAK2 tyrosine fcinase.
    • (1995) J Biol Chem , vol.270 , pp. 24292-24299
    • Prevarskaya, N.B.1    Skryma, R.M.2    Vacher, P.3    Daniel, N.4    Djiane, J.5    Duly, B.6
  • 43
    • 0027971438 scopus 로고
    • Calclum/calmodulln-dependent protein klnase II and potassium channel subuntt Eag similarly affect plasticity in Drosophito
    • Griffith LC, Wang J, Zhong Y, Wu C-F, Greenspan RJ; Calclum/calmodulln-dependent protein klnase II and potassium channel subuntt Eag similarly affect plasticity in Drosophito. Proc NatlAcad So' USA 1994, 91:10044-10048.
    • (1994) Proc NatlAcad So' USA , vol.91 , pp. 10044-10048
    • Griffith, L.C.1    Wang, J.2    Zhong, Y.3    Wu, C.-F.4    Greenspan, R.J.5
  • 44
    • 0029042633 scopus 로고
    • Klnase and phosphatase activities intimately associated with a reconstituted calcium-dependent potassium channel. 1
    • Calcium-activated potassium channels from rat brain were incorporated into lipid bilayers. The open probability of one class ol these channels was shown to be increased by addition of ATP. The effects of ATP could be mimicked by exogenous PKC or blocked by a PKC inhibitor. A phosphatase inhibitor potentiated the actions of ATP The résulta indicate that these channels are very tightly associated with an endogenous protein kinase and a phosphatase
    • Reinhart PH, Levitan IBKlnase and phosphatase activities intimately associated with a reconstituted calcium-dependent potassium channel. 1 Nevrosci 1995, 15:4572-4578. Calcium-activated potassium channels from rat brain were incorporated into lipid bilayers. The open probability of one class ol these channels was shown to be increased by addition of ATP. The effects of ATP could be mimicked by exogenous PKC or blocked by a PKC inhibitor. A phosphatase inhibitor potentiated the actions of ATP The résulta indicate that these channels are very tightly associated with an endogenous protein kinase and a phosphatase.
    • (1995) Nevrosci , vol.15 , pp. 4572-4578
    • Reinhart, P.H.1    Levitan, I.B.2
  • 45
    • 0028882810 scopus 로고
    • + channels by Interaction with a family of membrane-associated guanylate kinases
    • The clustering and localization of channels may be important for bringing them into proximity with kinases and phosphatases. In this study, clustering of potassium channels was shown to be induced by a class of proteins that includes the postsynaptic density protein PSD 95
    • + channels by Interaction with a family of membrane-associated guanylate kinases. Nature 1995, 378:85-88. The clustering and localization of channels may be important for bringing them into proximity with kinases and phosphatases. In this study, clustering of potassium channels was shown to be induced by a class of proteins that includes the postsynaptic density protein PSD 95.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.