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Volumn 25, Issue 30, 2005, Pages 6984-6996

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

Author keywords

Interaction domain; Subunit; Calcium channel; G protein; Neuron; Palmitoylation; Trafficking

Indexed keywords

ALANINE; CALCIUM CHANNEL N TYPE; DOPAMINE 2 RECEPTOR; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; QUINPIROLE; TRYPTOPHAN; VOLTAGE GATED CALCIUM CHANNEL;

EID: 23044516268     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.1137-05.2005     Document Type: Article
Times cited : (72)

References (43)
  • 3
    • 0024354817 scopus 로고
    • Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence
    • Bean BP (1989) Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence. Nature 340:153-156.
    • (1989) Nature , vol.340 , pp. 153-156
    • Bean, B.P.1
  • 8
    • 0034111386 scopus 로고    scopus 로고
    • Acidic motif responsible for plasma membrane association of the voltage-dependent calcium channel β1b subunit
    • Bogdanov Y, Brice NL, Canti C, Page KM, Li M, Volsen SG, Dolphin AC (2000) Acidic motif responsible for plasma membrane association of the voltage-dependent calcium channel β1b subunit. Eur J Neurosci 12: 894-902.
    • (2000) Eur J Neurosci , vol.12 , pp. 894-902
    • Bogdanov, Y.1    Brice, N.L.2    Canti, C.3    Page, K.M.4    Li, M.5    Volsen, S.G.6    Dolphin, A.C.7
  • 9
    • 0033566706 scopus 로고    scopus 로고
    • Identification of residues in the N terminus of α1B critical for inhibition of the voltage-dependent calcium channel by Gβγ
    • Canti C, Page KM, Stephens GJ, Dolphin AC (1999) Identification of residues in the N terminus of α1B critical for inhibition of the voltage-dependent calcium channel by Gβγ. J Neurosci 19:6855-6864.
    • (1999) J Neurosci , vol.19 , pp. 6855-6864
    • Canti, C.1    Page, K.M.2    Stephens, G.J.3    Dolphin, A.C.4
  • 10
    • 0034666058 scopus 로고    scopus 로고
    • Interaction between G proteins and accessory subunits in the regulation of α1B calcium channels in Xenopus oocytes
    • Canti C, Bogdanov Y, Dolphin AC (2000) Interaction between G proteins and accessory subunits in the regulation of α1B calcium channels in Xenopus oocytes. J Physiol (Lond) 527:419-432.
    • (2000) J Physiol (Lond) , vol.527 , pp. 419-432
    • Canti, C.1    Bogdanov, Y.2    Dolphin, A.C.3
  • 11
    • 0034872186 scopus 로고    scopus 로고
    • Evidence for two concentration-dependent processes for beta-subunit effects on α1B calcium channels
    • Canti C, Davies A, Berrow NS, Butcher AJ, Page KM, Dolphin AC (2001) Evidence for two concentration-dependent processes for beta-subunit effects on α1B calcium channels. Biophys J 81:1439-1451.
    • (2001) Biophys J , vol.81 , pp. 1439-1451
    • Canti, C.1    Davies, A.2    Berrow, N.S.3    Butcher, A.J.4    Page, K.M.5    Dolphin, A.C.6
  • 15
    • 0029967950 scopus 로고    scopus 로고
    • Identification of palmitoylation sites within the L-type calcium channel β2a subunit and effects on channel function
    • Chien AJ, Carr KM, Shirokov RE, Rios E, Hosey MM (1996) Identification of palmitoylation sites within the L-type calcium channel β2a subunit and effects on channel function. J Biol Chem 271:26465-26468.
    • (1996) J Biol Chem , vol.271 , pp. 26465-26468
    • Chien, A.J.1    Carr, K.M.2    Shirokov, R.E.3    Rios, E.4    Hosey, M.M.5
  • 20
    • 0345185172 scopus 로고    scopus 로고
    • Beta subunits of voltage-gated calcium channels
    • Dolphin AC (2003a) 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
  • 21
    • 0344197075 scopus 로고    scopus 로고
    • G protein modulation of voltage-gated calcium channels
    • Dolphin AC (2003b) G protein modulation of voltage-gated calcium channels. Pharmacol Rev 55:607-627.
    • (2003) Pharmacol Rev , vol.55 , pp. 607-627
    • Dolphin, A.C.1
  • 27
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits
    • Ikeda SR (1996) Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits. Nature 380:255-258.
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 28
    • 0031852755 scopus 로고    scopus 로고
    • Mechanism of auxiliary subunit modulation of neuronal alpha1E calcium channels
    • Jones LP, Wei SK, Yue DT (1998) Mechanism of auxiliary subunit modulation of neuronal alpha1E calcium channels. J Gen Physiol 112:125-143.
    • (1998) J Gen Physiol , vol.112 , pp. 125-143
    • Jones, L.P.1    Wei, S.K.2    Yue, D.T.3
  • 30
    • 0033868976 scopus 로고    scopus 로고
    • Calcium channel β subunit promotes voltage-dependent modulation of α1B by Gβγ
    • Meir A, Bell DC, Stephens GJ, Page KM, Dolphin AC (2000) Calcium channel β subunit promotes voltage-dependent modulation of α1B by Gβγ. Biophys J 79:731-746.
    • (2000) Biophys J , vol.79 , pp. 731-746
    • Meir, A.1    Bell, D.C.2    Stephens, G.J.3    Page, K.M.4    Dolphin, A.C.5
  • 31
    • 2542472258 scopus 로고    scopus 로고
    • Folding of active calcium channel β1b-subunit by size-exclusion chromatography and its role on channel function
    • Neely A, Garcia-Olivares J, Voswinkel S, Horstkott H, Hidalgo P (2004) Folding of active calcium channel β1b-subunit by size-exclusion chromatography and its role on channel function. J Biol Chem 279:21689-21694.
    • (2004) J Biol Chem , vol.279 , pp. 21689-21694
    • Neely, A.1    Garcia-Olivares, J.2    Voswinkel, S.3    Horstkott, H.4    Hidalgo, P.5
  • 32
    • 0028605745 scopus 로고
    • The amino terminus of a calcium channel β subunit sets rates of channel inactivation independently of the subunit's effect on activation
    • Olcese R, Qin N, Schneider T, Neely A, Wei X, Stefani E, Birnbaumer L (1994) The amino terminus of a calcium channel β subunit sets rates of channel inactivation independently of the subunit's effect on activation. Neuron 13:1433-1438.
    • (1994) Neuron , vol.13 , pp. 1433-1438
    • Olcese, R.1    Qin, N.2    Schneider, T.3    Neely, A.4    Wei, X.5    Stefani, E.6    Birnbaumer, L.7
  • 33
    • 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
  • 34
    • 0028179146 scopus 로고
    • Calcium channel β-subunit binds to a conserved motif in the I-II cytoplasmic linker of the α1-subunit
    • Pragnell M, De Waard M, Mori Y, Tanabe T, Snutch TP, Campbell KP (1994) Calcium channel β-subunit binds to a conserved motif in the I-II cytoplasmic linker of the α1-subunit. Nature 368:67-70.
    • (1994) Nature , vol.368 , pp. 67-70
    • Pragnell, M.1    De Waard, M.2    Mori, Y.3    Tanabe, T.4    Snutch, T.P.5    Campbell, K.P.6
  • 40
    • 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 (Lond) 525:377-390.
    • (2000) J Physiol (Lond) , vol.525 , pp. 377-390
    • Stephens, G.J.1    Page, K.M.2    Bogdanov, Y.3    Dolphin, A.C.4
  • 41
    • 2942615325 scopus 로고    scopus 로고
    • Structure of a complex between a voltage-gated calcium channel β-subunit and an alpha-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 alpha-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.