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Volumn 289, Issue 15, 2014, Pages 10387-10398

The N-terminal Domain Tethers the Voltage-gated Calcium Channel α2e-subunit to the Plasma Membrane via Electrostatic and Hydrophobic Interactions

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CALCIUM; CELL MEMBRANES; ELECTROSTATICS; IONIC STRENGTH; LIPID BILAYERS; LIPOSOMES; TETHERLINES;

EID: 84898634973     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.507244     Document Type: Article
Times cited : (29)

References (37)
  • 2
    • 0345185172 scopus 로고    scopus 로고
    • βSubunits of voltage-gated calcium channels
    • Dolphin, A. C. (2003) βsubunits of voltage-gated calcium channels. J. Bioenerg. Biomembr. 35, 599-620
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 599-620
    • Dolphin, A.C.1
  • 3
    • 34547931685 scopus 로고    scopus 로고
    • Multiplicity of protein interactions and functions of the voltage-gated calcium channel β-subunit
    • Hidalgo, P., and Neely, A. (2007) Multiplicity of protein interactions and functions of the voltage-gated calcium channel β-subunit. Cell Calcium 42, 389-396
    • (2007) Cell Calcium , vol.42 , pp. 389-396
    • Hidalgo, P.1    Neely, A.2
  • 5
    • 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, C. C., Campbell, K. P., and Hirsch, J. A. (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
  • 6
    • 2942615325 scopus 로고    scopus 로고
    • Structure of a complex between a voltage-gated calcium channel β-subunit and an β-subunit domain
    • Van Petegem, F., Clark, K. A., Chatelain, F. C., and Minor, D. L., Jr. (2004) Structure of a complex between a voltage-gated calcium channel β-subunit and an β-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
  • 7
    • 0038298772 scopus 로고    scopus 로고
    • Distinctive modulatory effects of five human auxiliary α2 subunit splice variants on L-type calcium channel gating
    • Takahashi, S. X., Mittman, S., and Colecraft, H. M. (2003) Distinctive modulatory effects of five human auxiliary α2 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
  • 8
    • 71049157923 scopus 로고    scopus 로고
    • Diversity and developmental expression of L-type calcium channel α2 proteins and their influence on calcium current in murine heart
    • Link, S., Meissner, M., Held, B., Beck, A., Weissgerber, P., Freichel, M., and Flockerzi, V. (2009) Diversity and developmental expression of L-type calcium channel α2 proteins and their influence on calcium current in murine heart. J. Biol. Chem. 284, 30129-30137
    • (2009) J. Biol. Chem. , vol.284 , pp. 30129-30137
    • Link, S.1    Meissner, M.2    Held, B.3    Beck, A.4    Weissgerber, P.5    Freichel, M.6    Flockerzi, V.7
  • 9
    • 0032483333 scopus 로고    scopus 로고
    • Membrane targeting of L-type calcium channels. Role of palmitoylation in the subcellular localization of the α2a subunit
    • Chien, A. J., Gao, T., Perez-Reyes, E., and Hosey, M. M. (1998) Membrane targeting of L-type calcium channels. Role of palmitoylation in the subcellular localization of the α2a subunit. J. Biol. Chem. 273, 23590-23597
    • (1998) J. Biol. Chem. , vol.273 , pp. 23590-23597
    • Chien, A.J.1    Gao, T.2    Perez-Reyes, E.3    Hosey, M.M.4
  • 10
    • 0028605745 scopus 로고
    • The amino termini of calcium channel β-subunits set rates of inactivation independently of their effect on activation
    • Olcese, R., Qin, N., Schneider, T., Neely, A., Wei, X., Stefani, E., and Birnbaumer, L. (1994) The amino termini of calcium channel β-subunits set rates of inactivation independently of their 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
  • 11
    • 33747646215 scopus 로고    scopus 로고
    • The α1-β subunit interaction that modulates calcium channel activity is reversible and requires a competentβ-interaction domain
    • Hidalgo, P., Gonzalez-Gutierrez, G., Garcia-Olivares, J., and Neely, A. (2006) The α1-β subunit interaction that modulates calcium channel activity is reversible and requires a competentβ-interaction domain. J. Biol. Chem. 281, 24104-24110
    • (2006) J. Biol. Chem. , vol.281 , pp. 24104-24110
    • Hidalgo, P.1    Gonzalez-Gutierrez, G.2    Garcia-Olivares, J.3    Neely, A.4
  • 14
    • 0029967950 scopus 로고    scopus 로고
    • Identification of palmitoylation sites within the L-type calcium channel α2a subunit and effects on channel function
    • Chien, A. J., Carr, K. M., Shirokov, R. E., Rios, E., and Hosey, M. M. (1996) Identification of palmitoylation sites within the L-type calcium channel α2a 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
  • 17
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and Cordelières, F. P. (2006) A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213-232
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 18
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 19
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao, D., and Wallace, B. A. (1984) Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23, 2667-2673
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 20
    • 0242380856 scopus 로고    scopus 로고
    • Extrusion technique to generate liposomes of defined size
    • Mui, B., Chow, L., and Hope, M. J. (2003) Extrusion technique to generate liposomes of defined size. Methods Enzymol. 367, 3-14
    • (2003) Methods Enzymol. , vol.367 , pp. 3-14
    • Mui, B.1    Chow, L.2    Hope, M.J.3
  • 21
    • 33748442138 scopus 로고    scopus 로고
    • 2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin i
    • 2+-triggered simultaneous membrane penetration of the tandem C2-domains of synaptotagmin I. Biophys. J. 91, 1767-1777
    • (2006) Biophys. J. , vol.91 , pp. 1767-1777
    • Hui, E.1    Bai, J.2    Chapman, E.R.3
  • 22
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • Burstein, E. A., and Emelyanenko, V. I. (1996) Log-normal description of fluorescence spectra of organic fluorophores. Photochem. Photobiol. 64, 316-320
    • (1996) Photochem. Photobiol. , vol.64 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.I.2
  • 23
    • 34447626465 scopus 로고    scopus 로고
    • Asimple fluorescence-spectroscopic membrane translocation assay
    • Keller, S., Böthe, M., Bienert, M., Dathe, M., and Blume, A. (2007)Asimple fluorescence-spectroscopic membrane translocation assay. Chembiochem 8, 546-552
    • (2007) Chembiochem , vol.8 , pp. 546-552
    • Keller, S.1    Böthe, M.2    Bienert, M.3    Dathe, M.4    Blume, A.5
  • 25
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize, A. L., Pogozheva, I. D., Lomize, M. A., and Mosberg, H. I. (2007) The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct. Biol. 7, 44
    • (2007) BMC Struct. Biol. , vol.7 , pp. 44
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 26
    • 0034877118 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
    • Reshetnyak, Y. K., Koshevnik, Y., and Burstein, E. A. (2001) Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues. Biophys. J. 81, 1735-1758
    • (2001) Biophys. J. , vol.81 , pp. 1735-1758
    • Reshetnyak, Y.K.1    Koshevnik, Y.2    Burstein, E.A.3
  • 27
    • 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, T. P., and Campbell, K. P. (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
  • 29
    • 33748881180 scopus 로고    scopus 로고
    • Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier
    • Sapay, N., Guermeur, Y., and Deléage, G. (2006) Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier. BMC Bioinformatics 7, 255
    • (2006) BMC Bioinformatics , vol.7 , pp. 255
    • Sapay, N.1    Guermeur, Y.2    Deléage, G.3
  • 30
    • 0026721333 scopus 로고
    • Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles
    • Chung, L. A., Lear, J. D., and DeGrado, W. F. (1992) Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles. Biochemistry 31, 6608-6616
    • (1992) Biochemistry , vol.31 , pp. 6608-6616
    • Chung, L.A.1    Lear, J.D.2    Degrado, W.F.3
  • 31
    • 0842323004 scopus 로고    scopus 로고
    • Functional roles of cytoplasmic loops and pore lining transmembrane helices in the voltage- dependent inactivation ofHVAcalcium channels
    • Stotz, S. C., Jarvis, S. E., and Zamponi, G. W. (2004) Functional roles of cytoplasmic loops and pore lining transmembrane helices in the voltage- dependent inactivation ofHVAcalcium channels. J. Physiol. 554, 263-273
    • (2004) J. Physiol. , vol.554 , pp. 263-273
    • Stotz, S.C.1    Jarvis, S.E.2    Zamponi, G.W.3
  • 32
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell, R. B., and Taneva, S. G. (2006) Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Curr. Protein Pept. Sci. 7, 539-552
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 33
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho, W., and Stahelin, R. V. (2005) Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34, 119-151
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 34
    • 7344252502 scopus 로고    scopus 로고
    • Post-translational modifications of β-subunits of voltage-dependent calcium channels
    • Chien, A. J., and Hosey, M. M. (1998) Post-translational modifications of β-subunits of voltage-dependent calcium channels. J. Bioenerg. Biomembr. 30, 377-386
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 377-386
    • Chien, A.J.1    Hosey, M.M.2
  • 36
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structurebased prediction of eukaryotic protein phosphorylation sites
    • Blom, N., Gammeltoft, S., and Brunak, S. (1999) Sequence and structurebased prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294, 1351-1362
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 37
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2


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