메뉴 건너뛰기




Volumn 289, Issue 14, 2014, Pages 9535-9546

A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BINDING ENERGY; IONS; LIGANDS; LIPID BILAYERS; MICELLES; SIGNAL TRANSDUCTION; THERMODYNAMICS;

EID: 84898067929     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.543389     Document Type: Article
Times cited : (12)

References (54)
  • 1
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp, U. B., and Seifert, R. (2002) Cyclic nucleotide-gated ion channels. Physiol. Rev. 82, 769-824
    • (2002) Physiol. Rev. , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 2
    • 0035047603 scopus 로고    scopus 로고
    • Molecular diversity of pacemaker ion channels
    • Kaupp, U. B., and Seifert, R. (2001) Molecular diversity of pacemaker ion channels. Annu. Rev. Physiol. 63, 235-257
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 235-257
    • Kaupp, U.B.1    Seifert, R.2
  • 3
    • 0012457490 scopus 로고    scopus 로고
    • Hyperpolarization-activated cation currents: From molecules to physiological function
    • Robinson, R. B., and Siegelbaum, S. A. (2003) Hyperpolarization-activated cation currents: from molecules to physiological function. Annu. Rev. Physiol. 65, 453-480
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 453-480
    • Robinson, R.B.1    Siegelbaum, S.A.2
  • 4
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen, G. (2002) The voltage-gated potassium channels and their relatives. Nature 419, 35-42
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 5
    • 0037264170 scopus 로고    scopus 로고
    • Overview of the voltage-gated sodium channel family
    • Yu, F. H., and Catterall, W. A. (2003) Overview of the voltage-gated sodium channel family. Genome Biol. 4, 207
    • (2003) Genome Biol. , vol.4 , pp. 207
    • Yu, F.H.1    Catterall, W.A.2
  • 6
    • 0026670519 scopus 로고
    • Cyclic nucleotide-binding domains in proteins having diverse functions
    • Shabb, J. B., and Corbin, J. D. (1992) Cyclic nucleotide-binding domains in proteins having diverse functions. J. Biol. Chem. 267, 5723-5726
    • (1992) J. Biol. Chem. , vol.267 , pp. 5723-5726
    • Shabb, J.B.1    Corbin, J.D.2
  • 7
    • 0029998701 scopus 로고    scopus 로고
    • Structure and function of cyclic nucleotide-gated channels
    • Zagotta, W. N., and Siegelbaum, S. A. (1996) Structure and function of cyclic nucleotide-gated channels. Annu. Rev. Neurosci. 19, 235-263
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 235-263
    • Zagotta, W.N.1    Siegelbaum, S.A.2
  • 8
    • 0032508040 scopus 로고    scopus 로고
    • A family of hyperpolarization-activated mammalian cation channels
    • Ludwig, A., Zong, X., Jeglitsch, M., Hofmann, F., and Biel, M. (1998) A family of hyperpolarization-activated mammalian cation channels. Nature 393, 587-591
    • (1998) Nature , vol.393 , pp. 587-591
    • Ludwig, A.1    Zong, X.2    Jeglitsch, M.3    Hofmann, F.4    Biel, M.5
  • 9
    • 0032577559 scopus 로고    scopus 로고
    • Identification of a gene encoding a hyperpolariza-tion-activated pacemaker channel of brain
    • Santoro, B., Liu, D. T., Yao, H., Bartsch, D., Kandel, E.R., Siegelbaum, S. A., and Tibbs, G. R. (1998) Identification of a gene encoding a hyperpolariza-tion-activated pacemaker channel of brain. Cell 93, 717-729
    • (1998) Cell , vol.93 , pp. 717-729
    • Santoro, B.1    Liu, D.T.2    Yao, H.3    Bartsch, D.4    Kandel, E.R.5    Siegelbaum, S.A.6    Tibbs, G.R.7
  • 10
    • 33645313112 scopus 로고    scopus 로고
    • CNG and HCN channels: Two peas, one pod
    • Craven, K. B., and Zagotta, W. N. (2006) CNG and HCN channels: two peas, one pod. Annu. Rev. Physiol. 68, 375-401
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 375-401
    • Craven, K.B.1    Zagotta, W.N.2
  • 11
    • 77954483652 scopus 로고    scopus 로고
    • Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels
    • Kusch, J., Biskup, C., Thon, S., Schulz, E., Nache, V., Zimmer, T., Schwede, F., and Benndorf, K. (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    Thon, S.3    Schulz, E.4    Nache, V.5    Zimmer, T.6    Schwede, F.7    Benndorf, K.8
  • 14
    • 79953875921 scopus 로고    scopus 로고
    • State-dependent cAMP binding to functioning HCN channels studied by patch clamp fluorometry
    • Wu, S., Vysotskaya, Z. V., Xu, X., Xie, C, Liu, Q., and Zhou, L. (2011) State-dependent cAMP binding to functioning HCN channels studied by patch clamp fluorometry. Biophys. J. 100, 1226-1232
    • (2011) Biophys. J. , vol.100 , pp. 1226-1232
    • Wu, S.1    Vysotskaya, Z.V.2    Xu, X.3    Xie, C.4    Liu, Q.5    Zhou, L.6
  • 15
    • 34249896932 scopus 로고    scopus 로고
    • Structure and rearrangements in the carboxy-terminal region of SpIH channels
    • Flynn, G. E., Black, K. D., Islas, L. D., Sankaran, B., and Zagotta, W. N. (2007) Structure and rearrangements in the carboxy-terminal region of SpIH channels. Structure 15, 671-682
    • (2007) Structure , vol.15 , pp. 671-682
    • Flynn, G.E.1    Black, K.D.2    Islas, L.D.3    Sankaran, B.4    Zagotta, W.N.5
  • 17
    • 67649604544 scopus 로고    scopus 로고
    • Mapping the structure and conformational movements of proteins with transition metal ion FRET
    • Taraska, J. W., Puljung, M. C., Olivier, N. B., Flynn, G. E., and Zagotta, W. N. (2009) Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nat. Methods 6, 532-537
    • (2009) Nat. Methods , vol.6 , pp. 532-537
    • Taraska, J.W.1    Puljung, M.C.2    Olivier, N.B.3    Flynn, G.E.4    Zagotta, W.N.5
  • 18
    • 78449237959 scopus 로고    scopus 로고
    • Structural basis for the cAMP-dependent gating in the human HCN4 channel
    • Xu, X., Vysotskaya, Z. V., Liu, Q., and Zhou, L. (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    Liu, Q.3    Zhou, L.4
  • 19
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta, W. N, Olivier, N. B., Black, K. D., Young, E. C., Olson, R., and Gouaux, E. (2003) Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425, 200-205
    • (2003) Nature , vol.425 , 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
  • 21
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417, 515-522
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    Mackinnon, R.6
  • 23
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf, H, Schmidt, O., Kümmerlen, R., Hinnah, S., Müller, D., Betzler, M., Steinkamp, T., and Wagner, R. (1995) A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans.EMBOJ. 14, 5170-5178
    • (1995) EMBOJ. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kümmerlen, R.3    Hinnah, S.4    Müller, D.5    Betzler, M.6    Steinkamp, T.7    Wagner, R.8
  • 24
    • 8844263765 scopus 로고    scopus 로고
    • Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel
    • Clayton, G. M., Silverman, W. R., Heginbotham, L., and Morais-Cabral, J. H. (2004) Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119, 615-627
    • (2004) Cell , vol.119 , pp. 615-627
    • Clayton, G.M.1    Silverman, W.R.2    Heginbotham, L.3    Morais-Cabral, J.H.4
  • 28
    • 79955011398 scopus 로고    scopus 로고
    • Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel
    • Schünke, S., Stoldt, M., Lecher, J., Kaupp, U. B., and Willbold, D. (2011) Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. Proc. Natl. Acad. Sci. U.S.A. 108, 6121-6126
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 6121-6126
    • Schünke, S.1    Stoldt, M.2    Lecher, J.3    Kaupp, U.B.4    Willbold, D.5
  • 29
    • 67650064749 scopus 로고    scopus 로고
    • Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP
    • Schünke, S., Stoldt, M., Novak, K., Kaupp, U. B., and Willbold, D. (2009) Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP. EMBORep. 10, 729-735
    • (2009) EMBORep. , vol.10 , pp. 729-735
    • Schünke, S.1    Stoldt, M.2    Novak, K.3    Kaupp, U.B.4    Willbold, D.5
  • 30
    • 34548402962 scopus 로고    scopus 로고
    • The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 Å resolution
    • Chiu, P. L., Pagel, M. D., Evans, J., Chou, H. T., Zeng, X., Gipson, B., Stahlberg, H., and Nimigean, C. M. (2007) The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 Å resolution. Structure 15, 1053-1064
    • (2007) Structure , vol.15 , pp. 1053-1064
    • Chiu, P.L.1    Pagel, M.D.2    Evans, J.3    Chou, H.T.4    Zeng, X.5    Gipson, B.6    Stahlberg, H.7    Nimigean, C.M.8
  • 32
    • 40849130624 scopus 로고    scopus 로고
    • Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles
    • Banerjee, S., Huber, T., and Sakmar, T. P. (2008) Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles. J. Mol. Biol. 377, 1067-1081
    • (2008) J. Mol. Biol. , vol.377 , pp. 1067-1081
    • Banerjee, S.1    Huber, T.2    Sakmar, T.P.3
  • 33
    • 79951634554 scopus 로고    scopus 로고
    • Non-vesicular transfer of membrane proteins from nanoparticles to lipid bilayers
    • Banerjee, S., and Nimigean, C. M. (2011) Non-vesicular transfer of membrane proteins from nanoparticles to lipid bilayers. J. Gen. Physiol. 137, 217-223
    • (2011) J. Gen. Physiol. , vol.137 , pp. 217-223
    • Banerjee, S.1    Nimigean, C.M.2
  • 37
    • 34547598211 scopus 로고    scopus 로고
    • Ligand binding and activation in a prokaryotic cyclic nucleotide-modulated channel
    • Nimigean, C. M., and Pagel, M. D. (2007) Ligand binding and activation in a prokaryotic cyclic nucleotide-modulated channel. J. Mol. Biol. 371, 1325-1337
    • (2007) J. Mol. Biol. , vol.371 , pp. 1325-1337
    • Nimigean, C.M.1    Pagel, M.D.2
  • 39
    • 0029745419 scopus 로고    scopus 로고
    • Nonequilibrium gating and voltage dependence of the ClC-0 Cl" channel
    • Chen, T. Y., and Miller, C. (1996) Nonequilibrium gating and voltage dependence of the ClC-0 Cl" channel. J. Gen. Physiol. 108, 237-250
    • (1996) J. Gen. Physiol. , vol.108 , pp. 237-250
    • Chen, T.Y.1    Miller, C.2
  • 40
    • 84901737014 scopus 로고    scopus 로고
    • Regulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectroflurorimetric assay
    • Rusinova, R., Kim, D. M., Nimigean, C. M., and Andersen, O. S. (2014) Regulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectroflurorimetric assay. Biophys. J. 106, 1070-1078
    • (2014) Biophys. J. , vol.106 , pp. 1070-1078
    • Rusinova, R.1    Kim, D.M.2    Nimigean, C.M.3    Andersen, O.S.4
  • 41
    • 77956403619 scopus 로고    scopus 로고
    • Screening for small molecules' bilayer-modifying potential using a gramicidin-based fluorescence assay
    • Ingolfsson, H. I., and Andersen, O.S. (2010) Screening for small molecules' bilayer-modifying potential using a gramicidin-based fluorescence assay. Assay Drug Dev. Technol. 8, 427-436
    • (2010) Assay Drug Dev. Technol. , vol.8 , pp. 427-436
    • Ingolfsson, H.I.1    Andersen, O.S.2
  • 42
    • 84890251336 scopus 로고    scopus 로고
    • Molecular interactions involved in proton-dependent gating in KcsA potassium channels
    • Posson, D. J., Thompson, A. N, McCoy, J. G., and Nimigean, C. M. (2013) Molecular interactions involved in proton-dependent gating in KcsA potassium channels. J. Gen. Physiol. 142, 613-624
    • (2013) J. Gen. Physiol. , vol.142 , pp. 613-624
    • Posson, D.J.1    Thompson, A.N.2    McCoy, J.G.3    Nimigean, C.M.4
  • 45
    • 80455155192 scopus 로고    scopus 로고
    • Role of the KcsA channel cytoplasmic domain in pH-dependent gating
    • Hirano, M., Onishi, Y., Yanagida, T., and Ide, T. (2011) Role of the KcsA channel cytoplasmic domain in pH-dependent gating. Biophys. J. 101, 2157-2162
    • (2011) Biophys. J. , vol.101 , pp. 2157-2162
    • Hirano, M.1    Onishi, Y.2    Yanagida, T.3    Ide, T.4
  • 46
    • 0032508032 scopus 로고    scopus 로고
    • Molecular identification of a hyperpolarization-activated channel in sea urchin sperm
    • Gauss, R., Seifert, R., and Kaupp, U. B. (1998) Molecular identification of a hyperpolarization-activated channel in sea urchin sperm. Nature 393, 583-587
    • (1998) Nature , vol.393 , pp. 583-587
    • Gauss, R.1    Seifert, R.2    Kaupp, U.B.3
  • 47
    • 0033529867 scopus 로고    scopus 로고
    • Molecular characterization of a slowly gating human hyper-polarization- activated channel predominantly expressed in thalamus, heart, and testis
    • Seifert, R., Scholten, A., Gauss, R., Mincheva, A., Lichter, P., and Kaupp, U. B. (1999) Molecular characterization of a slowly gating human hyper-polarization-activated channel predominantly expressed in thalamus, heart, and testis. Proc. Natl. Acad. Sci. U.S.A. 96, 9391-9396
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9391-9396
    • Seifert, R.1    Scholten, A.2    Gauss, R.3    Mincheva, A.4    Lichter, P.5    Kaupp, U.B.6
  • 48
    • 84855271367 scopus 로고    scopus 로고
    • Energetics of cyclic AMP binding to HCN channel C terminus reveal negative cooperativity
    • Chow, S. S., Van Petegem, F., and Accili, E. A. (2012) Energetics of cyclic AMP binding to HCN channel C terminus reveal negative cooperativity. J. Biol. Chem. 287, 600-606
    • (2012) J. Biol. Chem. , vol.287 , pp. 600-606
    • Chow, S.S.1    Van Petegem, F.2    Accili, E.A.3
  • 50
    • 65249169367 scopus 로고    scopus 로고
    • Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation
    • Quick, M., Winther, A. M., Shi, L., Nissen, P., Weinstein, H., and Javitch, J. A. (2009) Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation. Proc. Natl. Acad. Sci. U.S.A. 106, 5563-5568
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5563-5568
    • Quick, M.1    Winther, A.M.2    Shi, L.3    Nissen, P.4    Weinstein, H.5    Javitch, J.A.6
  • 51
    • 17044400911 scopus 로고    scopus 로고
    • A gate in the selectivity filter of potassium channels
    • Bernèche, S., and Roux, B. (2005) A gate in the selectivity filter of potassium channels. Structure 13, 591-600
    • (2005) Structure , vol.13 , pp. 591-600
    • Bernèche, S.1    Roux, B.2
  • 52
    • 29144472228 scopus 로고    scopus 로고
    • Activation-coupled inactivation in the bacterial potassium channel KcsA
    • Gao, L., Mi, X., Paajanen, V., Wang, K., and Fan, Z. (2005) Activation-coupled inactivation in the bacterial potassium channel KcsA. Proc. Natl. Acad. Sci. U.S.A. 102, 17630-17635
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 17630-17635
    • Gao, L.1    Mi, X.2    Paajanen, V.3    Wang, K.4    Fan, Z.5
  • 53
    • 77957267220 scopus 로고    scopus 로고
    • Am-phiphile regulation of ion channel function by changes in the bilayer spring constant
    • Lundbaek, J. A., Koeppe, R. E., 2nd, and Andersen, O. S. (2010) Am-phiphile regulation of ion channel function by changes in the bilayer spring constant. Proc. Natl. Acad. Sci. U.S.A. 107, 15427-15430.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15427-15430
    • Lundbaek, J.A.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 54
    • 84872123461 scopus 로고    scopus 로고
    • Kinetics of ligand-receptor interaction reveals an induced-fit mode of binding in a cyclic nucleotide-activated protein
    • Peuker, S., Cukkemane, A., Held, M., Noé, F., Kaupp, U. B., and Seifert, R. (2013) Kinetics of ligand-receptor interaction reveals an induced-fit mode of binding in a cyclic nucleotide-activated protein. Biophys. J. 104, 63-74
    • (2013) Biophys. J. , vol.104 , pp. 63-74
    • Peuker, S.1    Cukkemane, A.2    Held, M.3    Noé, F.4    Kaupp, U.B.5    Seifert, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.