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Volumn 3, Issue 10, 2008, Pages

Orientation of the calcium channel β relative to the α 12.2 subunit is critical for its regulation of channel activity

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CALCIUM CHANNEL SUBUNIT ALPHA1; GLYCINE; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED CALCIUM CHANNEL BETA; CACNA1B PROTEIN, HUMAN; CALCIUM CHANNEL L TYPE; CALCIUM CHANNEL N TYPE; PROTEIN SUBUNIT;

EID: 55849094732     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003560     Document Type: Article
Times cited : (26)

References (57)
  • 1
    • 0032531818 scopus 로고    scopus 로고
    • Calcium-a life and death signal
    • Berridge MJ, Bootman MD, Lipp P (1998) Calcium-a life and death signal. Nature 395: 645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 3
    • 0025775195 scopus 로고
    • Primary structure and functional expression from complementary DNA of a brain calcium channel
    • Mori Y, Friedrich T, Kim MS, Mikami A, Nakai J, et al. (1991) Primary structure and functional expression from complementary DNA of a brain calcium channel. Nature 350: 398-402.
    • (1991) Nature , vol.350 , pp. 398-402
    • Mori, Y.1    Friedrich, T.2    Kim, M.S.3    Mikami, A.4    Nakai, J.5
  • 4
    • 0025942910 scopus 로고
    • The roles of the subunits in the function of the calcium channel
    • Singer D, Biel M, Lotan I, Flockerzi V, Hofmann F, et al. (1991) The roles of the subunits in the function of the calcium channel. Science 253: 1553-1557.
    • (1991) Science , vol.253 , pp. 1553-1557
    • Singer, D.1    Biel, M.2    Lotan, I.3    Flockerzi, V.4    Hofmann, F.5
  • 8
    • 2942615325 scopus 로고    scopus 로고
    • Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain
    • Van Petegem F, Clark KA, Chatelain FC, Minor DL Jr (2004) Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain. Nature 429: 671-675.
    • (2004) Nature , vol.429 , pp. 671-675
    • Van Petegem, F.1    Clark, K.A.2    Chatelain, F.C.3    Minor Jr, D.L.4
  • 10
    • 2342666133 scopus 로고    scopus 로고
    • Structural analysis of the voltage-dependent calcium channel β subunit functional core and its complex with the α1 interaction domain
    • Opatowsky Y, Chen CC, Campbell KP, Hirsch JA (2004) Structural analysis of the voltage-dependent calcium channel β subunit functional core and its complex with the α1 interaction domain. Neuron 42: 387-399.
    • (2004) Neuron , vol.42 , pp. 387-399
    • Opatowsky, Y.1    Chen, C.C.2    Campbell, K.P.3    Hirsch, J.A.4
  • 13
  • 17
    • 1842686186 scopus 로고    scopus 로고
    • v2.2) calcium channel currents through a hyperpolarizing shift of ultra-slow and closed-state inactivation
    • v2.2) calcium channel currents through a hyperpolarizing shift of ultra-slow and closed-state inactivation. J Gen Physiol 123: 401-416.
    • (2004) J Gen Physiol , vol.123 , pp. 401-416
    • Yasuda, T.1    Lewis, R.J.2    Adams, D.J.3
  • 18
    • 0345185172 scopus 로고    scopus 로고
    • Beta subunits of voltage-gated calcium channels
    • Dolphin AC (2003) Beta subunits of voltage-gated calcium channels. J Bioenerg Biomembr 35: 599-620.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 599-620
    • Dolphin, A.C.1
  • 23
    • 0023101235 scopus 로고
    • Gating of Na channels. Inactivation modifiers discriminate among models
    • Gonoi T, Hille B (1987) Gating of Na channels. Inactivation modifiers discriminate among models. J Gen Physiol 89: 253-274.
    • (1987) J Gen Physiol , vol.89 , pp. 253-274
    • Gonoi, T.1    Hille, B.2
  • 25
    • 17644433239 scopus 로고    scopus 로고
    • The neuronal β4 subunit increases the unitary conductance of L-type voltage-gated calcium channels in PC12 cells
    • Schjott JM, Hsu SC, Plummer MR (2003) The neuronal β4 subunit increases the unitary conductance of L-type voltage-gated calcium channels in PC12 cells. J Biol Chem 278: 33936-33942.
    • (2003) J Biol Chem , vol.278 , pp. 33936-33942
    • Schjott, J.M.1    Hsu, S.C.2    Plummer, M.R.3
  • 26
    • 0027485912 scopus 로고
    • Human neuronal voltage-dependent calcium channels: Studies on subunit structure and role in channel assembly
    • Brust PF, Simerson S, Mccue AF, Deal CR, Schoonmaker S, et al. (1993) Human neuronal voltage-dependent calcium channels: studies on subunit structure and role in channel assembly. Neuropharmacology 32: 1089-1102.
    • (1993) Neuropharmacology , vol.32 , pp. 1089-1102
    • Brust, P.F.1    Simerson, S.2    Mccue, A.F.3    Deal, C.R.4    Schoonmaker, S.5
  • 29
    • 34347222583 scopus 로고    scopus 로고
    • Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells
    • Kerppola TK (2006) Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells. Nat Protoc 1: 1278-1286.
    • (2006) Nat Protoc , vol.1 , pp. 1278-1286
    • Kerppola, T.K.1
  • 30
    • 23044516268 scopus 로고    scopus 로고
    • Interaction via a key tryptophan in the I-II linker of N-type calcium channels is required for β1 but not for palmitoylated β2, implicating an additional binding site in the regulation of channel voltage-dependent properties
    • Leroy J, Richards MS, Butcher AJ, Nieto-Rostro M, Pratt WS, et al. (2005) Interaction via a key tryptophan in the I-II linker of N-type calcium channels is required for β1 but not for palmitoylated β2, implicating an additional binding site in the regulation of channel voltage-dependent properties. J Neurosci 25: 6984-6996.
    • (2005) J Neurosci , vol.25 , pp. 6984-6996
    • Leroy, J.1    Richards, M.S.2    Butcher, A.J.3    Nieto-Rostro, M.4    Pratt, W.S.5
  • 31
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu YJ, Liu H, Deng X, Hu CD (2006) Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. Biotechniques 40: 61-66.
    • (2006) Biotechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.D.4
  • 32
    • 84944811856 scopus 로고
    • A further contribution regarding the influence of the different constituents of the blood on the contraction of the heart
    • Ringer S (1883) A further contribution regarding the influence of the different constituents of the blood on the contraction of the heart. J Physiol 4: 29-42.
    • (1883) J Physiol , vol.4 , pp. 29-42
    • Ringer, S.1
  • 34
    • 0023850808 scopus 로고
    • Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit
    • Leung AT, Imagawa T, Block B, Franzini-Armstrong C, Campbell KP (1988) Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit. Journal of Biological Chemistry 263: 994-1001.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 994-1001
    • Leung, A.T.1    Imagawa, T.2    Block, B.3    Franzini-Armstrong, C.4    Campbell, K.P.5
  • 36
    • 0038045158 scopus 로고    scopus 로고
    • Auxiliary subunits: Essential components of the voltage-gated calcium channel complex
    • Arikkath J, Campbell KP (2003) Auxiliary subunits: essential components of the voltage-gated calcium channel complex. Curr Opin Neurobiol 13: 298-307.
    • (2003) Curr Opin Neurobiol , vol.13 , pp. 298-307
    • Arikkath, J.1    Campbell, K.P.2
  • 40
    • 0037207469 scopus 로고    scopus 로고
    • Molecular physiology of low-voltage-activated T-type calcium channels
    • Perez-Reyes E (2003) Molecular physiology of low-voltage-activated T-type calcium channels. Physiol Rev 83: 117-161.
    • (2003) Physiol Rev , vol.83 , pp. 117-161
    • Perez-Reyes, E.1
  • 43
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C, Deleage G (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 11: 681-684.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 44
    • 0029837127 scopus 로고    scopus 로고
    • Identification of a second region of the β-subunit involved in regulation of calcium channel inactivation
    • Qin N, Olcese R, Zhou J, Cabello OA, Birnbaumer L, et al. (1996) Identification of a second region of the β-subunit involved in regulation of calcium channel inactivation. American Journal of Physiology 271: C1539-1545.
    • (1996) American Journal of Physiology , vol.271
    • Qin, N.1    Olcese, R.2    Zhou, J.3    Cabello, O.A.4    Birnbaumer, L.5
  • 46
    • 0038298772 scopus 로고    scopus 로고
    • Distinctive modulatory effects of five human auxiliary β2 subunit splice variants on L-type calcium channel gating
    • Takahashi SX, Mittman S, Colecraft HM (2003) Distinctive modulatory effects of five human auxiliary β2 subunit splice variants on L-type calcium channel gating. Biophys J 84: 3007-3021.
    • (2003) Biophys J , vol.84 , pp. 3007-3021
    • Takahashi, S.X.1    Mittman, S.2    Colecraft, H.M.3
  • 48
    • 1942437417 scopus 로고    scopus 로고
    • Ca β-subunit displacement is a key step to induce the reluctant state of P/Q calcium channels by direct G protein regulation
    • Sandoz G, Lopez-Gonzalez I, Grunwald D, Bichet D, Altafaj X, et al. (2004) Ca β-subunit displacement is a key step to induce the reluctant state of P/Q calcium channels by direct G protein regulation. Proc Natl Acad Sci U S A 101: 6267-6272.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6267-6272
    • Sandoz, G.1    Lopez-Gonzalez, I.2    Grunwald, D.3    Bichet, D.4    Altafaj, X.5
  • 49
    • 0037155898 scopus 로고    scopus 로고
    • Geib S, Sandoz G, Cornet V, Mabrouk K, Fund-Saunier O, et al. (2002) The interaction between the I-II loop and the III-IV loop of Ca;2.1 contributes to voltage-dependent inactivation in a β-dependent manner. J Biol Chem 277: 10003-10013.
    • Geib S, Sandoz G, Cornet V, Mabrouk K, Fund-Saunier O, et al. (2002) The interaction between the I-II loop and the III-IV loop of Ca;2.1 contributes to voltage-dependent inactivation in a β-dependent manner. J Biol Chem 277: 10003-10013.
  • 53
    • 0035977069 scopus 로고    scopus 로고
    • Calcium channel β subunits differentially regulate the inhibition of N-type channels by individual Gβ isoforms
    • Feng Z-P, Arnot MI, Doering CJ, Zamponi GW (2001) Calcium channel β subunits differentially regulate the inhibition of N-type channels by individual Gβ isoforms. J Biol Chem 276: 45051-45058.
    • (2001) J Biol Chem , vol.276 , pp. 45051-45058
    • Feng, Z.-P.1    Arnot, M.I.2    Doering, C.J.3    Zamponi, G.W.4
  • 54
    • 0034213446 scopus 로고    scopus 로고
    • 2+ channel amino terminus contributes determinants for β subunit-mediated voltage-dependent inactivation properties
    • 2+ channel amino terminus contributes determinants for β subunit-mediated voltage-dependent inactivation properties. J Physiol 525 Pt 2: 377-390.
    • (2000) J Physiol , vol.525 , Issue.PART 2 , pp. 377-390
    • Stephens, G.J.1    Page, K.M.2    Bogdanov, Y.3    Dolphin, A.C.4
  • 56
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, et al. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22: 1567-1572.
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5
  • 57
    • 34548515291 scopus 로고    scopus 로고
    • X-ray structure of cerulean GFP: A tryptophan-based chromophore useful for fluorescence lifetime imaging
    • Malo GD, Pouwels LJ, Wang M, Weichsel A, Montfort WR, et al. (2007) X-ray structure of cerulean GFP: a tryptophan-based chromophore useful for fluorescence lifetime imaging. Biochemistry 46: 9865-9873.
    • (2007) Biochemistry , vol.46 , pp. 9865-9873
    • Malo, G.D.1    Pouwels, L.J.2    Wang, M.3    Weichsel, A.4    Montfort, W.R.5


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