메뉴 건너뛰기




Volumn 2, Issue 1, 2011, Pages

Lipid-dependent gating of a voltage-gated potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CHOLESTEROL; ION; LIPID; MEMBRANE PROTEIN; PHOSPHOLIPID; VOLTAGE GATED POTASSIUM CHANNEL; ARCHAEAL PROTEIN; ARGININE; CYSTEINE; RECOMBINANT PROTEIN;

EID: 79953236295     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1254     Document Type: Article
Times cited : (76)

References (60)
  • 2
    • 0038752614 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1038/nature01581
    • Jiang, Y., Ruta, V., Chen, J., Lee, A. & MacKinnon, R. The principle of gating charge movement in a voltage-dependent K+ channel. Nature 423, 42-48 (2003). (Pubitemid 36569578)
    • (2003) Nature , vol.423 , Issue.6935 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    MacKinnon, R.5
  • 3
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • DOI 10.1038/nature03888
    • Chanda, B., Asamoah, O. K., Blunck, R., Roux, B. & Bezanilla, F. Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement. Nature 436, 852-856 (2005). (Pubitemid 41160644)
    • (2005) Nature , vol.436 , Issue.7052 , pp. 852-856
    • Chanda, B.1    Asamoah, O.K.2    Blunck, R.3    Roux, B.4    Bezanilla, F.5
  • 4
    • 33846688821 scopus 로고    scopus 로고
    • The twisted ion-permeation pathway of a resting voltage-sensing domain
    • DOI 10.1038/nature05396, PII NATURE05396
    • Tombola, F., Pathak, M. M., Gorostiza, P. & Isacoff, E. Y. The twisted ionpermeation pathway of a resting voltage-sensing domain. Nature 445, 546-549 (2007). (Pubitemid 46197635)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 546-549
    • Tombola, F.1    Pathak, M.M.2    Gorostiza, P.3    Isacoff, E.Y.4
  • 6
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K. J. Sensing voltage across lipid membranes. Nature 456, 891-897 (2008).
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 8
    • 15244355809 scopus 로고    scopus 로고
    • Voltage-gated ion channels
    • DOI 10.1109/TNB.2004.842463
    • Bezanilla, F. Voltage-gated ion channels. IEEE Trans. Nanobioscience 4, 34-48 (2005). (Pubitemid 40384645)
    • (2005) IEEE Transactions on Nanobioscience , vol.4 , Issue.1 , pp. 34-48
    • Bezanilla, F.1
  • 9
    • 33846694346 scopus 로고    scopus 로고
    • Structure prediction for the down state of a potassium channel voltage sensor
    • DOI 10.1038/nature05494, PII NATURE05494
    • Grabe, M., Lai, H. C., Jain, M., Jan, Y. N. & Jan, L. Y. Structure prediction for the down state of a potassium channel voltage sensor. Nature 445, 550-553 (2007). (Pubitemid 46197636)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 550-553
    • Grabe, M.1    Lai, H.C.2    Jain, M.3    Nung Jan, Y.4    Yeh Jan, L.5
  • 10
    • 0032693966 scopus 로고    scopus 로고
    • Voltage sensitivity and gating charge in Shaker and Shab family potassium channels
    • Islas, L. D. & Sigworth, F. J. Voltage sensitivity and gating charge in Shaker and Shab family potassium channels. J. Gen. Physiol. 114, 723-742 (1999).
    • (1999) J. Gen. Physiol. , vol.114 , pp. 723-742
    • Islas, L.D.1    Sigworth, F.J.2
  • 11
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • Aggarwal, S. K. & MacKinnon, R. Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16, 1169-1177 (1996). (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 12
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., McCormack, K., Tanouye, M. A. & Sigworth, F. J. The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715 (1992).
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 13
    • 0030175867 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80142-7
    • Seoh, S. A., Sigg, D., Papazian, D. M. & Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron 16, 1159-1167 (1996). (Pubitemid 26227237)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1159-1167
    • Seoh, S.-A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 14
    • 0030731887 scopus 로고    scopus 로고
    • Probing the outer vestibule of a sodium channel voltage sensor
    • Yang, N., George, A. L. Jr & Horn, R. Probing the outer vestibule of a sodium channel voltage sensor. Biophys. J. 73, 2260-2268 (1997). (Pubitemid 27471438)
    • (1997) Biophysical Journal , vol.73 , Issue.5 , pp. 2260-2268
    • Yang, N.1    George Jr., A.L.2    Horn, R.3
  • 15
    • 0030070436 scopus 로고    scopus 로고
    • Transmembrane movement of the shaker K+ channel S4
    • Larsson, H. P., Baker, O. S., Dhillon, D. S. & Isacoff, E. Y. Transmembrane movement of the shaker K+ channel S4. Neuron 16, 387-397 (1996).
    • (1996) Neuron , vol.16 , pp. 387-397
    • Larsson, H.P.1    Baker, O.S.2    Dhillon, D.S.3    Isacoff, E.Y.4
  • 16
    • 13244272072 scopus 로고    scopus 로고
    • Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores
    • DOI 10.1016/j.neuron.2004.12.047, PII S0896627305000188
    • Tombola, F., Pathak, M. M. & Isacoff, E. Y. Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores. Neuron 45, 379-388 (2005). (Pubitemid 40188206)
    • (2005) Neuron , vol.45 , Issue.3 , pp. 379-388
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 17
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla, F. The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 80, 555-592 (2000). (Pubitemid 30164943)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 555-592
    • Bezanilla, F.1
  • 18
    • 0031877384 scopus 로고    scopus 로고
    • + channels in open, closed, and inactivated conformations
    • DOI 10.1006/jsbi.1998.3962
    • Durell, S. R., Hao, Y. & Guy, H. R. Structural models of the transmembrane region of voltage-gated and other K+ channels in open, closed, and inactivated conformations. J. Struct. Biol. 121, 263-284 (1998). (Pubitemid 28361451)
    • (1998) Journal of Structural Biology , vol.121 , Issue.2 , pp. 263-284
    • Durell, S.R.1    Hao, Y.2    Guy, H.R.3
  • 20
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1126/science.1116269
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903 (2005). (Pubitemid 41099919)
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 21
    • 3543107260 scopus 로고    scopus 로고
    • Localization of the voltage-sensor toxin receptor on KvAP
    • DOI 10.1021/bi049463y
    • Ruta, V. & MacKinnon, R. Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry 43, 10071-10079 (2004). (Pubitemid 39030898)
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10071-10079
    • Ruta, V.1    MacKinnon, R.2
  • 22
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376-382 (2007). (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 23
    • 77955626630 scopus 로고    scopus 로고
    • A shaker K+ channel with a miniature engineered voltage sensor
    • Xu, Y., Ramu, Y. & Lu, Z. A shaker K+ channel with a miniature engineered voltage sensor. Cell 142, 580-589 (2010).
    • (2010) Cell , vol.142 , pp. 580-589
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 25
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • Lee, A. G. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666, 62-87 (2004). (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 26
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan, W. & Bogdanov, M. Lipid-dependent membrane protein topogenesis. Annu. Rev. Biochem. 78, 515-540 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 27
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. & Simons, K. Lipid rafts as a membrane-organizing principle. Science 327, 46-50 (2010).
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 28
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • DOI 10.1146/annurev.biochem.67.1.199
    • Anderson, R. G. The caveolae membrane system. Annu. Rev. Biochem. 67, 199-225 (1998). (Pubitemid 28411129)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 29
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • DOI 10.1146/annurev.biophys.32.110601.142439
    • Edidin, M. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32, 257-283 (2003). (Pubitemid 37056230)
    • (2003) Annual Review of Biophysics and Biomolecular Structure , vol.32 , pp. 257-283
    • Edidin, M.1
  • 30
    • 21044449616 scopus 로고    scopus 로고
    • Targeting of voltage-gated potassium channel isoforms to distinct cell surface microdomains
    • DOI 10.1242/jcs.02348
    • O'Connell, K. M. & Tamkun, M. M. Targeting of voltage-gated potassium channel isoforms to distinct cell surface microdomains. J. Cell Sci. 118, 2155-2166 (2005). (Pubitemid 40872838)
    • (2005) Journal of Cell Science , vol.118 , Issue.10 , pp. 2155-2166
    • O'Connell, K.M.S.1    Tamkun, M.M.2
  • 33
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • DOI 10.1038/nature05416, PII NATURE05416
    • Schmidt, D., Jiang, Q. X. & MacKinnon, R. Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444, 775-779 (2006). (Pubitemid 44949608)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 34
    • 39149109885 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1038/nature06618, PII NATURE06618
    • Xu, Y., Ramu, Y. & Lu, Z. Removal of phospho-head groups of membrane lipids immobilizes voltage sensors of K+ channels. Nature 451, 826-829 (2008). (Pubitemid 351253175)
    • (2008) Nature , vol.451 , Issue.7180 , pp. 826-829
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 35
    • 33747062707 scopus 로고    scopus 로고
    • Enzymatic activation of voltage-gated potassium channels
    • DOI 10.1038/nature04880, PII NATURE04880
    • Ramu, Y., Xu, Y. & Lu, Z. Enzymatic activation of voltage-gated potassium channels. Nature 442, 696-699 (2006). (Pubitemid 44215325)
    • (2006) Nature , vol.442 , Issue.7103 , pp. 696-699
    • Ramu, Y.1    Xu, Y.2    Lu, Z.3
  • 37
    • 0031952461 scopus 로고    scopus 로고
    • Activation of Shaker potassium channels: III. An activation gating model for wild-type and V2 mutant channels
    • DOI 10.1085/jgp.111.2.313
    • Schoppa, N. E. & Sigworth, F. J. Activation of Shaker potassium channels III: An activation gating model for wild-type and V2 mutant channels. J. Gen. Physiol. 111, 313-342 (1998). (Pubitemid 28113080)
    • (1998) Journal of General Physiology , vol.111 , Issue.2 , pp. 313-342
    • Schoppa, N.E.1    Sigworth, F.J.2
  • 38
    • 0028140472 scopus 로고
    • Shaker potassium channel gating III: Evaluation of kinetic models for activation
    • Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Shaker potassium channel gating. III: evaluation of kinetic models for activation. J. Gen. Physiol. 103, 321-362 (1994). (Pubitemid 24068562)
    • (1994) Journal of General Physiology , vol.103 , Issue.2 , pp. 321-362
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 39
    • 0037015161 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1021/bi026215y
    • Valiyaveetil, F. I., Zhou, Y. & MacKinnon, R. Lipids in the structure, folding, and function of the KcsA K+ channel. Biochemistry 41 (35), 10771-10777 (2002). (Pubitemid 34971053)
    • (2002) Biochemistry , vol.41 , Issue.35 , pp. 10771-10777
    • Valiyaveetil, F.I.1    Zhou, Y.2    MacKinnon, R.3
  • 40
    • 0028106688 scopus 로고
    • + channels
    • Sun, T., Naini, A. A. & Miller, C. High-level expression and functional reconstitution of Shaker K+ channels. Biochemistry 33, 9992-9999 (1994). (Pubitemid 24286076)
    • (1994) Biochemistry , vol.33 , Issue.33 , pp. 9992-9999
    • Sun, T.1    Naini, A.A.2    Miller, C.3
  • 41
    • 3843056748 scopus 로고    scopus 로고
    • Can shaker potassium channels be locked in the deactivated state?
    • DOI 10.1085/jgp.200409057
    • Yang, Y., Yan, Y. & Sigworth, F. J. Can Shaker potassium channels be locked in the deactivated state? J. Gen. Physiol. 124, 163-171 (2004). (Pubitemid 39038190)
    • (2004) Journal of General Physiology , vol.124 , Issue.2 , pp. 163-171
    • Yang, Y.1    Yan, Y.2    Sigworth, F.J.3
  • 42
    • 27544516349 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/j.cell.2005.08.041, PII S0092867405009128
    • Ruta, V., Chen, J. & MacKinnon, R. Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel. Cell 123, 463-475 (2005). (Pubitemid 41546676)
    • (2005) Cell , vol.123 , Issue.3 , pp. 463-475
    • Ruta, V.1    Chen, J.2    MacKinnon, R.3
  • 43
    • 0041695463 scopus 로고    scopus 로고
    • Answers and questions from the KvAP structures
    • DOI 10.1016/S0896-6273(03)00472-0
    • Cohen, B. E., Grabe, M. & Jan, L. Y. Answers and questions from the KvAP structures. Neuron 39, 395-400 (2003). (Pubitemid 36937042)
    • (2003) Neuron , vol.39 , Issue.3 , pp. 395-400
    • Cohen, B.E.1    Grabe, M.2    Jan, L.Y.3
  • 44
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • Jiang, Y. et al. X-ray structure of a voltage-dependent K+ channel. Nature 423, 33-41 (2003).
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 45
    • 34547628129 scopus 로고    scopus 로고
    • + channel in a membrane environment
    • DOI 10.1529/biophysj.107.112540
    • Jogini, V. & Roux, B. Dynamics of the Kv1.2 voltage-gated K+ channel in a membrane environment. Biophys. J. 93, 3070-3082 (2007). (Pubitemid 350097098)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 46
    • 1442333334 scopus 로고    scopus 로고
    • Specificity of charge-carrying residues in the voltage sensor of potassium channels
    • DOI 10.1085/jgp.200308993
    • Ahern, C. A. & Horn, R. Specificity of charge-carrying residues in the voltage sensor of potassium channels. J. Gen. Physiol. 123, 205-216 (2004). (Pubitemid 38282971)
    • (2004) Journal of General Physiology , vol.123 , Issue.3 , pp. 205-216
    • Ahern, C.A.1    Horn, R.2
  • 47
    • 0035039731 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1085/jgp.117.5.469
    • Starace, D. M. & Bezanilla, F. Histidine scanning mutagenesis of basic residues of the S4 segment of the shaker K+ channel. J. Gen. Physiol. 117, 469-490 (2001). (Pubitemid 32441397)
    • (2001) Journal of General Physiology , vol.117 , Issue.5 , pp. 469-490
    • Starace, D.M.1    Bezanilla, F.2
  • 48
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channels
    • Yang, N. & Horn, R. Evidence for voltage-dependent S4 movement in sodium channels. Neuron 15, 213-218 (1995).
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 52
    • 77952584138 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals
    • Hite, R. K., Li, Z. & Walz, T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 29, 1652-1658 (2010).
    • (2010) EMBO J. , vol.29 , pp. 1652-1658
    • Hite, R.K.1    Li, Z.2    Walz, T.3
  • 54
    • 78650476908 scopus 로고    scopus 로고
    • S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: Implications for detergent-solubilized membrane proteins
    • doi:10.1371/journal.pbio.1000555 [doi]
    • Dorwart, M. R., Wray, R., Brautigam, C. A., Jiang, Y. & Blount, P. S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins. PLoS Biol. 8, e1000555, doi:10.1371/journal.pbio.1000555 [doi] (2010).
    • (2010) PLoS Biol. , vol.8
    • Dorwart, M.R.1    Wray, R.2    Brautigam, C.A.3    Jiang, Y.4    Blount, P.5
  • 56
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • DOI 10.1126/science.1065635
    • Ren, D. et al. A prokaryotic voltage-gated sodium channel. Science 294, 2372-2375 (2001). (Pubitemid 33140564)
    • (2001) Science , vol.294 , Issue.5550 , pp. 2372-2375
    • Ren, D.1    Navarro, B.2    Xu, H.3    Yue, L.4    Shi, Q.5    Clapham, D.E.6
  • 57
    • 5144229327 scopus 로고    scopus 로고
    • Gating of the bacterial sodium channel, NaChBac: Voltage-dependent charge movement and gating currents
    • DOI 10.1085/jgp.200409139
    • Kuzmenkin, A., Bezanilla, F. & Correa, A. M. Gating of the bacterial sodium channel, NaChBac: voltage-dependent charge movement and gating currents. J. Gen. Physiol. 124, 349-356 (2004). (Pubitemid 39346639)
    • (2004) Journal of General Physiology , vol.124 , Issue.4 , pp. 349-356
    • Kuzmenkin, A.1    Bezanilla, F.2    Correa, A.M.3
  • 58
    • 4043151338 scopus 로고    scopus 로고
    • + channels in an open conformation
    • DOI 10.1038/nature02735
    • Jiang, Q. X., Wang, D. N. & MacKinnon, R. Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation. Nature 430, 806-810 (2004). (Pubitemid 39071354)
    • (2004) Nature , vol.430 , Issue.7001 , pp. 806-810
    • Jiang, Q.-X.1    Wang, D.-N.2    MacKinnon, R.3
  • 59
    • 0028173889 scopus 로고
    • Engineering a uniquely reactive thiol into a cysteine-rich peptide
    • Shimony, E., Sun, T., Kolmakova-Partensky, L. & Miller, C. Engineering a uniquely reactive thiol into a cysteine-rich peptide. Protein Eng. 7, 503-507 (1994). (Pubitemid 24106802)
    • (1994) Protein Engineering , vol.7 , Issue.4 , pp. 503-507
    • Shimony, E.1    Sun, T.2    Kolmakova-Partensky, L.3    Miller, C.4
  • 60
    • 62449219614 scopus 로고    scopus 로고
    • Biopanning of phage displayed peptide libraries for the isolation of cell-specific ligands
    • McGuire, M. J., Li, S. & Brown, K. C. Biopanning of phage displayed peptide libraries for the isolation of cell-specific ligands. Methods Mol. Biol. 504, 291-321 (2009).
    • (2009) Methods Mol. Biol. , vol.504 , pp. 291-321
    • McGuire, M.J.1    Li, S.2    Brown, K.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.