메뉴 건너뛰기




Volumn 287, Issue 24, 2012, Pages 20509-20521

Multiple cholesterol recognition/interaction amino acid consensus (CRAC) motifs in cytosolic C tail of Slo1 subunit determine cholesterol sensitivity of Ca2+- and voltage-gated K+ (BK) channels

Author keywords

[No Author keywords available]

Indexed keywords

ACTION POTENTIALS; BIOLOGICAL PROCESS; BK-CHANNEL; CHANNEL INTERACTIONS; CHANNEL PROTEINS; CONSENSUS MOTIF; CRAC MOTIF; CYTOSOLIC; ENDOTHELIAL FUNCTION; HYDROPHOBIC INTERACTIONS; ION CHANNEL; ION TRANSPORTS; MEMBRANE CHOLESTEROL; MEMBRANE-ASSOCIATED PROTEINS; PROTEIN SURFACE; SMOOTH MUSCLES; STRUCTURAL BASIS;

EID: 84862001785     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.356261     Document Type: Article
Times cited : (85)

References (56)
  • 1
    • 12344270987 scopus 로고    scopus 로고
    • What's so special about cholesterol?
    • DOI 10.1007/s11745-004-1336-x
    • Mouritsen, O. G., and Zuckermann, M. J. (2004) What's so special about cholesterol? Lipids 39, 1101-1113 (Pubitemid 40136615)
    • (2004) Lipids , vol.39 , Issue.11 , pp. 1101-1113
    • Mouritsen, O.G.1    Zuckermann, M.J.2
  • 2
    • 9644294471 scopus 로고    scopus 로고
    • Structural basis for lipid modulation of nicotinic acetylcholine receptor function
    • Barrantes, F. J. (2004) Structural basis for lipid modulation of nicotinic acetylcholine receptor function. Brain Res. Brain Res. Rev. 47, 71-95
    • (2004) Brain Res. Brain Res. Rev. , vol.47 , pp. 71-95
    • Barrantes, F.J.1
  • 3
    • 77952302051 scopus 로고    scopus 로고
    • Cholesterol effects on nicotinic acetylcholine receptor. Cellular aspects
    • Barrantes, F. J. (2010) Cholesterol effects on nicotinic acetylcholine receptor. Cellular aspects. Subcell. Biochem. 51, 467-487
    • (2010) Subcell. Biochem. , vol.51 , pp. 467-487
    • Barrantes, F.J.1
  • 4
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • Epand, R. M. (2006) Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45, 279-294
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 6
    • 78650919372 scopus 로고    scopus 로고
    • Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein-coupled receptors
    • Jafurulla, M., Tiwari, S., and Chattopadhyay, A. (2011) Identification of cholesterol recognition amino acid consensus (CRAC) motif in G-protein-coupled receptors. Biochem. Biophys. Res. Commun. 404, 569-573
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 569-573
    • Jafurulla, M.1    Tiwari, S.2    Chattopadhyay, A.3
  • 7
    • 84862016442 scopus 로고    scopus 로고
    • Differential contribution of BK subunits to nongenomic regulation of channel function by steroids
    • (Barrantes, F. J., and Levitan, I., eds) John Wiley & Sons, Inc., in press
    • Dopico, A. M., Bukiya, A. N., and Singh, A. K. (2012) Differential contribution of BK subunits to nongenomic regulation of channel function by steroids. in Cholesterol Regulation of Ion Channels and Receptors (Barrantes, F. J., and Levitan, I., eds) John Wiley & Sons, Inc., in press
    • (2012) Cholesterol Regulation of Ion Channels and Receptors
    • Dopico, A.M.1    Bukiya, A.N.2    Singh, A.K.3
  • 8
    • 24044542689 scopus 로고    scopus 로고
    • Inhibition of the calcium- and voltage-dependent big conductance potassium channel ameliorates cisplatin-induced apoptosis in spiral ligament fibrocytes of the cochlea
    • DOI 10.1016/j.neuroscience.2005.05.055, PII S030645220500521X
    • Liang, F., Schulte, B. A., Qu, C., Hu, W., and Shen, Z. (2005) Inhibition of the calcium- and voltage-dependent big conductance potassium channel ameliorates cisplatin-induced apoptosis in spiral ligament fibrocytes of the cochlea. Neuroscience 135, 263-271 (Pubitemid 41219754)
    • (2005) Neuroscience , vol.135 , Issue.1 , pp. 263-271
    • Liang, F.1    Schulte, B.A.2    Qu, C.3    Hu, W.4    Shen, Z.5
  • 10
    • 47749110251 scopus 로고    scopus 로고
    • An unexpected role for ion channels in brain tumor metastasis
    • Sontheimer, H. (2008) An unexpected role for ion channels in brain tumor metastasis. Exp. Biol. Med. 233, 779-791
    • (2008) Exp. Biol. Med. , vol.233 , pp. 779-791
    • Sontheimer, H.1
  • 12
    • 9644254296 scopus 로고    scopus 로고
    • Membrane cholesterol content modulates activation of BK channels in colonic epithelia
    • DOI 10.1016/j.bbamem.2004.11.004, PII S0005273604002895
    • Lam, R. S, Shaw A. R., and Duszyk, M. (2004) Membrane cholesterol content modulates activation of BK channels in colonic epithelia. Biochim. Biophys. Acta 1667, 241-248 (Pubitemid 39576089)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1667 , Issue.2 , pp. 241-248
    • Lam, R.S.1    Shaw, A.R.2    Duszyk, M.3
  • 13
    • 34249700573 scopus 로고    scopus 로고
    • 2+- activated component of outward potassium current and decreases membrane capacitance in rat uterine myocytes
    • 2+-activated component of outward potassium current and decreases membrane capacitance in rat uterine myocytes. J. Physiol. 581, 445-456
    • (2007) J. Physiol. , vol.581 , pp. 445-456
    • Shmygol, A.1    Noble, K.2    Wray, S.3
  • 17
  • 18
    • 77956012236 scopus 로고    scopus 로고
    • BK channel activation. Structural and functional insights
    • Lee, U. S., and Cui, J. (2010) BK channel activation. Structural and functional insights. Trends Neurosci. 33, 415-423
    • (2010) Trends Neurosci. , vol.33 , pp. 415-423
    • Lee, U.S.1    Cui, J.2
  • 19
    • 0028942821 scopus 로고
    • Attenuation of channel kinetics and conductance by cholesterol. An interpretation using structural stress as a unifying concept
    • Chang, H. M., Reitstetter, R., Mason, R. P., and Gruener, R. (1995) Attenuation of channel kinetics and conductance by cholesterol. An interpretation using structural stress as a unifying concept. J. Membr. Biol. 143, 51-63
    • (1995) J. Membr. Biol. , vol.143 , pp. 51-63
    • Chang, H.M.1    Reitstetter, R.2    Mason, R.P.3    Gruener, R.4
  • 23
    • 33847768020 scopus 로고    scopus 로고
    • Lipid stress at play. Mechanosensitivity of voltage-gated channels
    • Morris, C. E., and Juranka, P. F. (2007) Lipid stress at play. Mechanosensitivity of voltage-gated channels. Curr. Top. Membr. 59, 297-337
    • (2007) Curr. Top. Membr. , vol.59 , pp. 297-337
    • Morris, C.E.1    Juranka, P.F.2
  • 24
    • 42949098097 scopus 로고    scopus 로고
    • Lipid bilayer-mediated regulation of ion channel function by amphiphilic drugs
    • Lundbaek, J. A. (2008) Lipid bilayer-mediated regulation of ion channel function by amphiphilic drugs. J. Gen. Physiol. 131, 421-429
    • (2008) J. Gen. Physiol. , vol.131 , pp. 421-429
    • Lundbaek, J.A.1
  • 25
    • 78650905628 scopus 로고    scopus 로고
    • Specificity of cholesterol and analogs to modulate BK channels points to direct sterol-channel protein interactions
    • Bukiya, A. N., Belani, J. D., Rychnovsky, S., and Dopico, A. M. (2011) Specificity of cholesterol and analogs to modulate BK channels points to direct sterol-channel protein interactions. J. Gen. Physiol. 137, 93-110
    • (2011) J. Gen. Physiol. , vol.137 , pp. 93-110
    • Bukiya, A.N.1    Belani, J.D.2    Rychnovsky, S.3    Dopico, A.M.4
  • 30
    • 0038273863 scopus 로고    scopus 로고
    • Ca channels from arterial smooth muscle does not require the presence of the β1-subunit
    • Ca channels from arterial smooth muscle does not require the presence of the β1-subunit. Am. J. Physiol. Cell Physiol. 284, C1468-C1480
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Dopico, A.M.1
  • 33
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • DOI 10.1073/pnas.031461598
    • Li, H., Yao, Z., Degenhardt, B., Teper, G., and Papadopoulos, V. (2001) Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide. Proc. Natl. Acad. Sci. U.S.A. 98, 1267-1272 (Pubitemid 32121221)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.3 , pp. 1267-1272
    • Li, H.1    Yao, Z.-X.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 36
    • 0037028130 scopus 로고    scopus 로고
    • Capotassium channels lacking calcium bowl and RCK domains
    • Capotassium channels lacking calcium bowl and RCK domains. Nature 420, 499-502
    • (2002) Nature , vol.420 , pp. 499-502
    • Piskorowski, R.1    Aldrich, R.W.2
  • 37
    • 0037462823 scopus 로고    scopus 로고
    • + (MaxiK) channel is necessary for its cell surface expression
    • + (MaxiK) channel is necessary for its cell surface expression. J. Biol. Chem. 278, 2713-2722
    • (2003) J. Biol. Chem. , vol.278 , pp. 2713-2722
    • Wang, S.X.1    Ikeda, M.2    Guggino, W.B.3
  • 39
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains. An overview
    • Epand, R. M., Thomas, A., Brasseur, R., and Epand, R. F. (2010) Cholesterol interaction with proteins that partition into membrane domains. An overview. Subcell. Biochem. 51, 253-278
    • (2010) Subcell. Biochem. , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 40
    • 77952313405 scopus 로고    scopus 로고
    • Cholesterol-protein interaction. Methods and cholesterol reporter molecules
    • Gimpl, G. (2010) Cholesterol-protein interaction. Methods and cholesterol reporter molecules. Subcell. Biochem. 51, 1-45
    • (2010) Subcell. Biochem. , vol.51 , pp. 1-45
    • Gimpl, G.1
  • 42
    • 20444438852 scopus 로고    scopus 로고
    • 2+-binding sites, multiple sites, multiple ions
    • 2+-binding sites, multiple sites, multiple ions. J. Gen. Physiol. 125, 253-255
    • (2005) J. Gen. Physiol. , vol.125 , pp. 253-255
    • Cox, D.H.1
  • 45
    • 67049158432 scopus 로고    scopus 로고
    • Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase
    • Edwards, A. A., Mason, J. M., Clinch, K., Tyler, P. C., Evans, G. B., and Schramm, V. L. (2009) Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase. Biochemistry 48, 5226-5238
    • (2009) Biochemistry , vol.48 , pp. 5226-5238
    • Edwards, A.A.1    Mason, J.M.2    Clinch, K.3    Tyler, P.C.4    Evans, G.B.5    Schramm, V.L.6
  • 47
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • DOI 10.1016/S0005-2736(02)00611-9, PII S0005273602006119
    • Vincent, N., Genin, C., and Malvoisin, E. (2002) Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups. Biochim. Biophys. Acta 1567, 157-164 (Pubitemid 35454057)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1567 , Issue.SUPPL. , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 48
    • 37049016678 scopus 로고    scopus 로고
    • Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines
    • DOI 10.1158/0008-5472.CAN-07-1771
    • Palmer, C. P., Mahen, R., Schnell, E., Djamgoz, M. B., and Aydar, E. (2007) Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines. Cancer Res. 67, 11166-11175 (Pubitemid 350248541)
    • (2007) Cancer Research , vol.67 , Issue.23 , pp. 11166-11175
    • Palmer, C.P.1    Mahen, R.2    Schnell, E.3    Djamgoz, M.B.A.4    Aydar, E.5
  • 49
    • 33847786718 scopus 로고    scopus 로고
    • Cytoplasmic domain of human myelin protein zero likely folded as β-structure in compact myelin
    • DOI 10.1529/biophysj.106.094722
    • Luo, X., Sharma, D., Inouye, H., Lee, D., Avila, R. L., Salmona, M., and Kirschner, D. A. (2007) Cytoplasmic domain of human myelin protein zero likely folded as β-structure in compact myelin. Biophys. J. 92, 1585-1597 (Pubitemid 46393469)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1585-1597
    • Luo, X.1    Sharma, D.2    Inouye, H.3    Lee, D.4    Avila, R.L.5    Salmona, M.6    Kirschner, D.A.7
  • 50
    • 66049119910 scopus 로고    scopus 로고
    • Cholesterol regulates the endoplasmic reticulum exit of the major membrane protein P0 required for peripheral myelin compaction
    • Saher, G., Quintes, S., Möbius, W., Wehr, M. C., Krämer-Albers, E. M., Brügger, B., and Nave, K. A. (2009) Cholesterol regulates the endoplasmic reticulum exit of the major membrane protein P0 required for peripheral myelin compaction. J. Neurosci. 29, 6094-6104
    • (2009) J. Neurosci. , vol.29 , pp. 6094-6104
    • Saher, G.1    Quintes, S.2    Möbius, W.3    Wehr, M.C.4    Krämer-Albers, E.M.5    Brügger, B.6    Nave, K.A.7
  • 51
    • 77952307606 scopus 로고    scopus 로고
    • Cholesterol and myelin biogenesis
    • Saher, G., and Simons, M. (2010) Cholesterol and myelin biogenesis. Subcell. Biochem. 51, 489-508
    • (2010) Subcell. Biochem. , vol.51 , pp. 489-508
    • Saher, G.1    Simons, M.2
  • 53
    • 67449090254 scopus 로고    scopus 로고
    • Cytolethal distending toxin-induced cell cycle arrest of lymphocytes is dependent upon recognition and binding to cholesterol
    • Boesze-Battaglia, K., Brown, A., Walker, L., Besack, D., Zekavat, A., Wrenn, S., Krummenacher, C., and Shenker, B. J. (2009) Cytolethal distending toxin-induced cell cycle arrest of lymphocytes is dependent upon recognition and binding to cholesterol. J. Biol. Chem. 284, 10650-10658
    • (2009) J. Biol. Chem. , vol.284 , pp. 10650-10658
    • Boesze-Battaglia, K.1    Brown, A.2    Walker, L.3    Besack, D.4    Zekavat, A.5    Wrenn, S.6    Krummenacher, C.7    Shenker, B.J.8
  • 54
    • 0030633451 scopus 로고    scopus 로고
    • Has nature designed the cholesterol side chain for optimal interaction with phospholipids?
    • Bittman, R. (1997) Has nature designed the cholesterol side chain for optimal interaction with phospholipids? Subcell. Biochem. 28, 145-171
    • (1997) Subcell. Biochem. , vol.28 , pp. 145-171
    • Bittman, R.1
  • 55
    • 0030892178 scopus 로고    scopus 로고
    • Dehydroergosterol structural organization in aqueous medium and in a model system of membranes
    • Loura, L. M., and Prieto, M. (1997) Dehydroergosterol structural organization in aqueous medium and in a model system of membranes. Biophys. J. 72, 2226-2236 (Pubitemid 27184450)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2226-2236
    • Loura, L.M.S.1    Prieto, M.2
  • 56
    • 33646182618 scopus 로고    scopus 로고
    • β2 and β4 subunits of BK channels confer differential sensitivity to acute modulation by steroid hormones
    • King, J. T., Lovell, P. V., Rishniw, M., Kotlikoff, M. I., Zeeman, M. L., and McCobb, D. P. (2006) β2 and β4 subunits of BK channels confer differential sensitivity to acute modulation by steroid hormones. J. Neurophysiol. 95, 2878-2888
    • (2006) J. Neurophysiol. , vol.95 , pp. 2878-2888
    • King, J.T.1    Lovell, P.V.2    Rishniw, M.3    Kotlikoff, M.I.4    Zeeman, M.L.5    McCobb, D.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.