메뉴 건너뛰기




Volumn 100, Issue 5, 2011, Pages 1226-1232

State-dependent cAMP binding to functioning HCN channels studied by patch-clamp fluorometry

Author keywords

[No Author keywords available]

Indexed keywords


EID: 79953875921     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.01.034     Document Type: Article
Times cited : (46)

References (48)
  • 1
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • DOI 10.1126/science.1108595
    • Changeux, J. P., and S. J. Edelstein. 2005. Allosteric mechanisms of signal transduction. Science. 308:1424-1428. (Pubitemid 40791288)
    • (2005) Science , vol.308 , Issue.5727 , pp. 1424-1428
    • Changeux, J.-P.1    Edelstein, S.J.2
  • 2
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl. Acad. Sci. USA. 44:98-104.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 3
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with protein-protein interactions
    • DOI 10.1016/j.sbi.2004.01.005
    • Goh, C. S., D. Milburn, and M. Gerstein. 2004. Conformational changes associated with protein-protein interactions. Curr. Opin. Struct. Biol. 14:104-109. (Pubitemid 38258244)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 104-109
    • Goh, C.-S.1    Milburn, D.2    Gerstein, M.3
  • 4
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., J. Wyman, and J. P. Changeux. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 5
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui, Q., and M. Karplus. 2008. Allostery and cooperativity revisited. Protein Sci. 17:1295-1307.
    • (2008) Protein Sci. , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 6
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • DOI 10.1038/nsb0197-10
    • Dill, K. A., and H. S. Chan. 1997. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19. (Pubitemid 27020916)
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 8
    • 71449103005 scopus 로고    scopus 로고
    • Hidden alternative structures of proline isomerase essential for catalysis
    • Fraser, J. S., M. W. Clarkson, T. Alber. 2009. Hidden alternative structures of proline isomerase essential for catalysis. Nature. 462:669-673.
    • (2009) Nature , vol.462 , pp. 669-673
    • Fraser, J.S.1    Clarkson, M.W.2    Alber, T.3
  • 10
    • 0030959460 scopus 로고    scopus 로고
    • Allosteric activation and tuning of ligand efficacy in cyclic- nucleotide-gated channels
    • DOI 10.1038/386612a0
    • Tibbs, G. R., E. H. Goulding, and S. A. Siegelbaum. 1997. Allosteric activation and tuning of ligand efficacy in cyclic-nucleotide-gated channels. Nature. 386:612-615. (Pubitemid 27175427)
    • (1997) Nature , vol.386 , Issue.6625 , pp. 612-615
    • Tibbs, G.R.1    Goulding, E.H.2    Siegelbaum, S.A.3
  • 11
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. 1998. Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 125:924-947.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 13
    • 0023657765 scopus 로고
    • Molecular neurobiology. Channel families in the brain
    • Stevens, C. F. 1987. Molecular neurobiology. Channel families in the brain. Nature. 328:198-199.
    • (1987) Nature , vol.328 , pp. 198-199
    • Stevens, C.F.1
  • 14
  • 15
    • 67651030760 scopus 로고    scopus 로고
    • Hyperpolarization-activated cation channels: From genes to function
    • Biel, M., C. Wahl-Schott, X. Zong. 2009. Hyperpolarization-activated cation channels: from genes to function. Physiol. Rev. 89: 847-885.
    • (2009) Physiol. Rev. , vol.89 , pp. 847-885
    • Biel, M.1    Wahl-Schott, C.2    Zong, X.3
  • 16
    • 0027530224 scopus 로고
    • Pacemaker mechanisms in cardiac tissue
    • DiFrancesco, D. 1993. Pacemaker mechanisms in cardiac tissue. Annu. Rev. Physiol. 55:455-472.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 455-472
    • Difrancesco, D.1
  • 17
    • 36148965480 scopus 로고    scopus 로고
    • The funny current: Cellular basis for the control of heart rate
    • DiFrancesco, D., and J. S. Borer. 2007. The funny current: cellular basis for the control of heart rate. Drugs. 67 (Suppl 2):15-24. (Pubitemid 350114592)
    • (2007) Drugs , vol.67 , Issue.SUPPL. 2 , pp. 15-24
    • DiFrancesco, D.1    Borer, J.S.2
  • 18
    • 0012457490 scopus 로고    scopus 로고
    • Hyperpolarization-Activated Cation Currents: From Molecules to Physiological Function
    • DOI 10.1146/annurev.physiol.65.092101.142734
    • Robinson, R. B., and S. A. Siegelbaum. 2003. Hyperpolarization-activated cation currents: from molecules to physiological function. Annu. Rev. Physiol. 65:453-480. (Pubitemid 38249163)
    • (2003) Annual Review of Physiology , vol.65 , pp. 453-480
    • Robinson, R.B.1    Siegelbaum, S.A.2
  • 19
    • 0347302947 scopus 로고    scopus 로고
    • Changes in Local S4 Environment Provide a Voltage-sensing Mechanism for Mammalian Hyperpolarization-activated HCN Channels
    • DOI 10.1085/jgp.200308918
    • Bell, D. C., H. Yao, . , S. A. Siegelbaum. 2004. Changes in local S4 environment provide a voltage-sensing mechanism for mammalian hyperpolarization-activated HCN channels. J. Gen. Physiol. 123:5-19. (Pubitemid 38082783)
    • (2004) Journal of General Physiology , vol.123 , Issue.1 , pp. 5-19
    • Bell, D.C.1    Yao, H.2    Saenger, R.C.3    Riley, J.H.4    Siegelbaum, S.A.5
  • 20
    • 0346041553 scopus 로고    scopus 로고
    • S4 Movement in a Mammalian HCN Channel
    • DOI 10.1085/jgp.200308916
    • Vemana, S., S. Pandey, and H. P. Larsson. 2004. S4 movement in a mammalian HCN channel. J. Gen. Physiol. 123:21-32. (Pubitemid 38082784)
    • (2004) Journal of General Physiology , vol.123 , Issue.1 , pp. 21-32
    • Vemana, S.1    Pandey, S.2    Larsson, H.P.3
  • 21
    • 0037167878 scopus 로고    scopus 로고
    • Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages
    • DOI 10.1038/nature01038
    • Männikkö, R., F. Elinder, and H. P. Larsson. 2002. Voltage-sensing mechanism is conserved among ion channels gated by opposite voltages. Nature. 419:837-841. (Pubitemid 35238569)
    • (2002) Nature , vol.419 , Issue.6909 , pp. 837-841
    • Mannikko, R.1    Elinder, F.2    Larsson, H.P.3
  • 22
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K. J. 2008. Sensing voltage across lipid membranes. Nature. 456:891-897.
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 23
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • DOI 10.1038/nature01922
    • Zagotta, W. N., N. B. Olivier, . , E. Gouaux. 2003. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature. 425:200-205. (Pubitemid 37150901)
    • (2003) Nature , vol.425 , Issue.6954 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 24
    • 0033104823 scopus 로고    scopus 로고
    • Dual allosteric modulation of pacemaker (F) channels by cAMP and voltage in rabbit SA node
    • DiFrancesco, D. 1999. Dual allosteric modulation of pacemaker (F) channels by cAMP and voltage in rabbit SA node. J. Physiol. 515:367-376.
    • (1999) J. Physiol. , vol.515 , pp. 367-376
    • Difrancesco, D.1
  • 25
    • 0347627834 scopus 로고    scopus 로고
    • Regulation of Hyperpolarization-Activated HCN Channels by cAMP through a Gating Switch in Binding Domain Symmetry
    • DOI 10.1016/S0896-6273(03)00753-0
    • Ulens, C., and S. A. Siegelbaum. 2003. Regulation of hyperpolarization- activated HCN channels by cAMP through a gating switch in binding domain symmetry. Neuron. 40:959-970. (Pubitemid 37522053)
    • (2003) Neuron , vol.40 , Issue.5 , pp. 959-970
    • Ulens, C.1    Siegelbaum, S.A.2
  • 26
    • 0037168125 scopus 로고    scopus 로고
    • Activity-dependent regulation of HCN pacemaker channels by cyclic AMP: Signaling through dynamic allosteric coupling
    • DOI 10.1016/S0896-6273(02)00968-6
    • Wang, J., S. Chen, . , S. A. Siegelbaum. 2002. Activity-dependent regulation of HCN pacemaker channels by cyclic AMP: signaling through dynamic allosteric coupling. Neuron. 36:451-461. (Pubitemid 35284732)
    • (2002) Neuron , vol.36 , Issue.3 , pp. 451-461
    • Wang, J.1    Chen, S.2    Nolan, M.F.3    Siegelbaum, S.A.4
  • 27
    • 77954483652 scopus 로고    scopus 로고
    • Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels
    • Kusch, J., C. Biskup, . , K. Benndorf. 2010. Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels. Neuron. 67:75-85.
    • (2010) Neuron , vol.67 , pp. 75-85
    • Kusch, J.1    Biskup, C.2    Benndorf, K.3
  • 30
    • 77952339435 scopus 로고    scopus 로고
    • Fluorescence applications in molecular neurobiology
    • Taraska, J. W., and W. N. Zagotta. 2010. Fluorescence applications in molecular neurobiology. Neuron. 66:170-189.
    • (2010) Neuron , vol.66 , pp. 170-189
    • Taraska, J.W.1    Zagotta, W.N.2
  • 31
    • 0037389277 scopus 로고    scopus 로고
    • Patch-clamp fluorometry recording of conformational rearrangements of ion channels
    • Zheng, J., and W. N. Zagotta. 2003. Patch-clamp fluorometry recording of conformational rearrangements of ion channels. Sci. STKE. 2003:PL7.
    • (2003) Sci. STKE. , vol.2003
    • Zheng, J.1    Zagotta, W.N.2
  • 32
    • 67449128707 scopus 로고    scopus 로고
    • Use of voltage clamp fluorimetry in understanding potassium channel gating: A review of Shaker fluorescence data
    • Horne, A. J., and D. Fedida. 2009. Use of voltage clamp fluorimetry in understanding potassium channel gating: a review of Shaker fluorescence data. Can. J. Physiol. Pharmacol. 87:411-418.
    • (2009) Can. J. Physiol. Pharmacol. , vol.87 , pp. 411-418
    • Horne, A.J.1    Fedida, D.2
  • 33
    • 0030840167 scopus 로고    scopus 로고
    • + channel with fluorescence
    • + channel with fluorescence. Neuron. 19:1127-1140. (Pubitemid 27512372)
    • (1997) Neuron , vol.19 , Issue.5 , pp. 1127-1140
    • Cha, A.1    Bezanilla, F.2
  • 34
    • 2942651050 scopus 로고    scopus 로고
    • Detecting rearrangements of Shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells
    • DOI 10.1529/biophysj.103.034512
    • Blunck, R., D. M. Starace, . , F. Bezanilla. 2004. Detecting rearrangements of Shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells. Biophys. J. 86:3966-3980. (Pubitemid 38780273)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3966-3980
    • Blunck, R.1    Starace, D.M.2    Correa, A.M.3    Bezanilla, F.4
  • 35
    • 78449237959 scopus 로고    scopus 로고
    • Structural basis for the cAMP-dependent gating in the human HCN4 channel
    • Xu, X., Z. V. Vysotskaya, . , L. Zhou. 2010. Structural basis for the cAMP-dependent gating in the human HCN4 channel. J. Biol. Chem. 285:37082-37091.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37082-37091
    • Xu, X.1    Vysotskaya, Z.V.2    Zhou, L.3
  • 36
    • 0032548836 scopus 로고    scopus 로고
    • A state-independent interaction between ligand and a conserved arginine residue in cyclic nucleotide-gated channels reveals a functional polarity of the cyclic nucleotide binding site
    • DOI 10.1074/jbc.273.8.4497
    • Tibbs, G. R., D. T. Liu, S. A. Siegelbaum. 1998. A state-independent interaction between ligand and a conserved arginine residue in cyclic nucleotide-gated channels reveals a functional polarity of the cyclic nucleotide binding site. J. Biol. Chem. 273:4497-4505. (Pubitemid 28103190)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.8 , pp. 4497-4505
    • Tibbs, G.R.1    Liu, D.T.2    Leypold, B.G.3    Siegelbaum, S.A.4
  • 37
    • 34249869012 scopus 로고    scopus 로고
    • Gating of HCN Channels by Cyclic Nucleotides: Residue Contacts that Underlie Ligand Binding, Selectivity, and Efficacy
    • DOI 10.1016/j.str.2007.04.012, PII S0969212607001797
    • Zhou, L., and S. A. Siegelbaum. 2007. Gating of HCN channels by cyclic nucleotides: residue contacts that underlie ligand binding, selectivity, and efficacy. Structure. 15:655-670. (Pubitemid 46874082)
    • (2007) Structure , vol.15 , Issue.6 , pp. 655-670
    • Zhou, L.1    Siegelbaum, S.A.2
  • 38
    • 1842740890 scopus 로고    scopus 로고
    • Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels: Molecular coupling between the S4-S5 and C-linkers
    • DOI 10.1074/jbc.M313704200
    • Decher, N., J. Chen, and M. C. Sanguinetti. 2004. Voltage-dependent gating of hyperpolarization-activated, cyclic nucleotide-gated pacemaker channels: molecular coupling between the S4-S5 and C-linkers. J. Biol. Chem. 279:13859-13865. (Pubitemid 38468918)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13859-13865
    • Decher, N.1    Chen, J.2    Sanguinetti, M.C.3
  • 39
    • 33846647992 scopus 로고    scopus 로고
    • Voltage sensor movement and cAMP binding allosterically regulate an inherently voltage-independent closed-open transition in HCN channels
    • DOI 10.1085/jgp.200609585
    • Chen, S., J. Wang, . , S. A. Siegelbaum. 2007. Voltage sensor movement and cAMP binding allosterically regulate an inherently voltageindependent closed-open transition in HCN channels. J. Gen. Physiol. 129:175-188. (Pubitemid 46184874)
    • (2007) Journal of General Physiology , vol.129 , Issue.2 , pp. 175-188
    • Chen, S.1    Wang, J.2    Zhou, L.3    George, M.S.4    Siegelbaum, S.A.5
  • 40
    • 37049032338 scopus 로고    scopus 로고
    • 2+ Spikes in Distal Dendrites of CA1 Pyramidal Neurons
    • DOI 10.1016/j.neuron.2007.11.015, PII S0896627307009671
    • Tsay, D., J. T. Dudman, and S. A. Siegelbaum. 2007. HCN1 channels constrain synaptically evoked Ca2+ spikes in distal dendrites of CA1 pyramidal neurons. Neuron. 56:1076-1089. (Pubitemid 350251121)
    • (2007) Neuron , vol.56 , Issue.6 , pp. 1076-1089
    • Tsay, D.1    Dudman, J.T.2    Siegelbaum, S.A.3
  • 41
    • 0018387132 scopus 로고
    • How does adrenaline accelerate the heart?
    • DOI 10.1038/280235a0
    • Brown, H. F., D. DiFrancesco, and S. J. Noble. 1979. How does adrenaline accelerate the heart? Nature. 280:235-236. (Pubitemid 9227914)
    • (1979) Nature , vol.280 , Issue.5719 , pp. 235-236
    • Brown, H.F.1    DiFrancesco, D.2    Noble, S.J.3
  • 42
    • 0025782740 scopus 로고
    • Direct activation of cardiac pacemaker channels by intracellular cyclic AMP
    • DiFrancesco, D., and P. Tortora. 1991. Direct activation of cardiac pacemaker channels by intracellular cyclic AMP. Nature. 351: 145-147. (Pubitemid 21896552)
    • (1991) Nature , vol.351 , Issue.6322 , pp. 145-147
    • DiFrancesco, D.1    Tortora, P.2
  • 43
    • 0033237837 scopus 로고    scopus 로고
    • Dendritic IH normalizes temporal summation in hippocampal CA1 neurons
    • Magee, J. C. 1999. Dendritic IH normalizes temporal summation in hippocampal CA1 neurons. Nat. Neurosci. 2:848.
    • (1999) Nat. Neurosci. , vol.2 , pp. 848
    • Magee, J.C.1
  • 44
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • Catterall, W. A. 2010. Ion channel voltage sensors: structure, function, and pathophysiology. Neuron. 67:915-928.
    • (2010) Neuron. , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 45
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • DOI 10.1038/nrm2376, PII NRM2376
    • Bezanilla, F. 2008. How membrane proteins sense voltage. Nat. Rev. Mol. Cell Biol. 9:323-332. (Pubitemid 351430853)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 323-332
    • Bezanilla, F.1
  • 47
    • 0036830645 scopus 로고    scopus 로고
    • Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism
    • DOI 10.1038/nn926
    • Chang, Y., and D. S. Weiss. 2002. Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism. Nat. Neurosci. 5:1163-1168. (Pubitemid 35247175)
    • (2002) Nature Neuroscience , vol.5 , Issue.11 , pp. 1163-1168
    • Chang, Y.1    Weiss, D.S.2
  • 48
    • 33745015539 scopus 로고    scopus 로고
    • A receptor
    • DOI 10.1021/bi060222v
    • Muroi, Y., C. Czajkowski, and M. B. Jackson. 2006. Local and global ligand-induced changes in the structure of the GABAA receptor. Biochemistry. 45:7013-7022. (Pubitemid 43877390)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7013-7022
    • Muroi, Y.1    Czajkowski, C.2    Jackson, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.