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Volumn 1768, Issue 1, 2007, Pages 39-51

Gating of the ATP-sensitive K+ channel by a pore-lining phenylalanine residue

Author keywords

Gating; Hydrophobicity; KATP channel; Kir6.2; Steric hindrance

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE SENSITIVE POTASSIUM CHANNEL; AMINO ACID; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR6.2; PHENYLALANINE; PROTON; TRYPTOPHAN;

EID: 33845396667     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.06.027     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 0021086270 scopus 로고
    • + channels in cardiac muscle
    • + channels in cardiac muscle. Nature 305 (1983) 147-148
    • (1983) Nature , vol.305 , pp. 147-148
    • Noma, A.1
  • 2
    • 0021187646 scopus 로고
    • + channels in pancreatic B-cells
    • + channels in pancreatic B-cells. Nature 311 (1984) 271-273
    • (1984) Nature , vol.311 , pp. 271-273
    • Cook, D.L.1    Hales, C.N.2
  • 3
    • 0023911193 scopus 로고
    • Adenosine 5′-triphosphate-sensitive potassium channels
    • Ashcroft F.M. Adenosine 5′-triphosphate-sensitive potassium channels. Annu. Rev. Neurosci. 11 (1988) 97-118
    • (1988) Annu. Rev. Neurosci. , vol.11 , pp. 97-118
    • Ashcroft, F.M.1
  • 4
    • 0032787462 scopus 로고    scopus 로고
    • + channels and insulin secretion: their role in health and disease
    • + channels and insulin secretion: their role in health and disease. Diabetologia 42 (1999) 903-919
    • (1999) Diabetologia , vol.42 , pp. 903-919
    • Ashcroft, F.M.1    Gribble, F.M.2
  • 5
    • 0030934798 scopus 로고    scopus 로고
    • Inward rectifier potassium channels
    • Nichols C.G., and Lopatin A.N. Inward rectifier potassium channels. Annu. Rev. Physiol. 59 (1997) 171-191
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 171-191
    • Nichols, C.G.1    Lopatin, A.N.2
  • 8
    • 0032491439 scopus 로고    scopus 로고
    • Membrane phospholipid control of nucleotide sensitivity of KATP channels
    • Shyng S.L., and Nichols C.G. Membrane phospholipid control of nucleotide sensitivity of KATP channels. Science 282 (1998) 1138-1141
    • (1998) Science , vol.282 , pp. 1138-1141
    • Shyng, S.L.1    Nichols, C.G.2
  • 9
    • 0025103305 scopus 로고
    • + channels in skeletal muscle by intracellular protons
    • + channels in skeletal muscle by intracellular protons. Nature 343 (1990) 375-377
    • (1990) Nature , vol.343 , pp. 375-377
    • Davies, N.W.1
  • 13
    • 2542464972 scopus 로고    scopus 로고
    • Structural changes during ion channel gating
    • Doyle D.A. Structural changes during ion channel gating. Trends Neurosci. 27 (2004) 298-302
    • (2004) Trends Neurosci. , vol.27 , pp. 298-302
    • Doyle, D.A.1
  • 14
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen G. The voltage-gated potassium channels and their relatives. Nature 419 (2002) 35-42
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 15
    • 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. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417 (2002) 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
  • 18
    • 22144481606 scopus 로고    scopus 로고
    • Structural locus of the pH gate in the Kir1.1 inward rectifier channel
    • Sackin H., Nanazashvili M., Palmer L.G., Krambis M., and Walters D.E. Structural locus of the pH gate in the Kir1.1 inward rectifier channel. Biophys. J. 88 (2005) 2597-2606
    • (2005) Biophys. J. , vol.88 , pp. 2597-2606
    • Sackin, H.1    Nanazashvili, M.2    Palmer, L.G.3    Krambis, M.4    Walters, D.E.5
  • 19
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • Sukharev S., Betanzos M., Chiang C.S., and Guy H.R. The gating mechanism of the large mechanosensitive channel MscL. Nature 409 (2001) 720-724
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.S.3    Guy, H.R.4
  • 20
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature 373 (1995) 37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 21
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • Unwin N. Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy. FEBS Lett. 555 (2003) 91-95
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 22
    • 0041766301 scopus 로고    scopus 로고
    • Protons activate homomeric Kir6.2 channels by selective suppression of the long and intermediate closures
    • Wu J., Xu H., Yang Z., Wang Y., Mao J., and Jiang C. Protons activate homomeric Kir6.2 channels by selective suppression of the long and intermediate closures. J. Membr. Biol. 190 (2002) 105-116
    • (2002) J. Membr. Biol. , vol.190 , pp. 105-116
    • Wu, J.1    Xu, H.2    Yang, Z.3    Wang, Y.4    Mao, J.5    Jiang, C.6
  • 26
    • 0000410893 scopus 로고
    • The principles of the stochastic interpretation of ion-channel mechanisms
    • Sakmann B., and Neher E. (Eds), Plenum Press, New York
    • Colquhoun D., and Hawkes A.G. The principles of the stochastic interpretation of ion-channel mechanisms. In: Sakmann B., and Neher E. (Eds). Single-Channel Recording (1995), Plenum Press, New York 397-482
    • (1995) Single-Channel Recording , pp. 397-482
    • Colquhoun, D.1    Hawkes, A.G.2
  • 27
    • 0031713173 scopus 로고    scopus 로고
    • Molecular analysis of ATP-sensitive K channel gating and implications for channel inhibition by ATP
    • Trapp S., Proks P., Tucker S.J., and Ashcroft F.M. Molecular analysis of ATP-sensitive K channel gating and implications for channel inhibition by ATP. J. Gen. Physiol. 112 (1998) 333-349
    • (1998) J. Gen. Physiol. , vol.112 , pp. 333-349
    • Trapp, S.1    Proks, P.2    Tucker, S.J.3    Ashcroft, F.M.4
  • 30
    • 0034161609 scopus 로고    scopus 로고
    • Regulation of ATP-sensitive potassium channel function by protein kinase A-mediated phosphorylation in transfected HEK293 cells
    • Lin Y.F., Jan Y.N., and Jan L.Y. Regulation of ATP-sensitive potassium channel function by protein kinase A-mediated phosphorylation in transfected HEK293 cells. EMBO J. 19 (2000) 942-955
    • (2000) EMBO J. , vol.19 , pp. 942-955
    • Lin, Y.F.1    Jan, Y.N.2    Jan, L.Y.3
  • 33
    • 1642537864 scopus 로고
    • +-induced anomalous rectification in squid giant axons
    • +-induced anomalous rectification in squid giant axons. J. Gen. Physiol. 273 (1966) F516-F529
    • (1966) J. Gen. Physiol. , vol.273
    • Armstrong, C.M.1
  • 34
    • 0034977038 scopus 로고    scopus 로고
    • Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels
    • Flynn G.E., and Zagotta W.N. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron 30 (2001) 689-698
    • (2001) Neuron , vol.30 , pp. 689-698
    • Flynn, G.E.1    Zagotta, W.N.2
  • 35
    • 0035974844 scopus 로고    scopus 로고
    • Rotational movement during cyclic nucleotide-gated channel opening
    • Johnson Jr. J.P., and Zagotta W.N. Rotational movement during cyclic nucleotide-gated channel opening. Nature 412 (2001) 917-921
    • (2001) Nature , vol.412 , pp. 917-921
    • Johnson Jr., J.P.1    Zagotta, W.N.2
  • 38
    • 0035025069 scopus 로고    scopus 로고
    • Blocker state dependence and trapping in hyperpolarization-activated cation channels: evidence for an intracellular activation gate
    • Shin K.S., Rothberg B.S., and Yellen G. Blocker state dependence and trapping in hyperpolarization-activated cation channels: evidence for an intracellular activation gate. J. Gen. Physiol. 117 (2001) 91-101
    • (2001) J. Gen. Physiol. , vol.117 , pp. 91-101
    • Shin, K.S.1    Rothberg, B.S.2    Yellen, G.3
  • 39
    • 0034123344 scopus 로고    scopus 로고
    • Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel
    • Capener C.E., Shrivastava I.H., Ranatunga K.M., Forrest L.R., Smith G.R., and Sansom M.S. Homology modeling and molecular dynamics simulation studies of an inward rectifier potassium channel. Biophys. J. 78 (2000) 2929-2942
    • (2000) Biophys. J. , vol.78 , pp. 2929-2942
    • Capener, C.E.1    Shrivastava, I.H.2    Ranatunga, K.M.3    Forrest, L.R.4    Smith, G.R.5    Sansom, M.S.6
  • 40
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 41
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3 (1996) 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 42
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.