메뉴 건너뛰기




Volumn 105, Issue 46, 2008, Pages 17795-17800

Two protonation switches control rhodopsin activation in membranes

Author keywords

FTIR spectroscopy; G protein coupled receptor; Ionic lock; Membrane protein; UV visible spectroscopy

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CARBOXYLIC ACID; GLUTAMIC ACID; RHODOPSIN;

EID: 56649097496     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0804541105     Document Type: Article
Times cited : (135)

References (41)
  • 1
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P, Cotecchia S, Costa T, Lefkowitz RJ (1993) A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J Biol Chem 268:4625-4636.
    • (1993) J Biol Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 2
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: Structural basis of molecular physiology
    • Menon ST, Han M, Sakmar TP (2001) Rhodopsin: Structural basis of molecular physiology. Physiol Rev 81:1659-1688.
    • (2001) Physiol Rev , vol.81 , pp. 1659-1688
    • Menon, S.T.1    Han, M.2    Sakmar, T.P.3
  • 3
    • 0034051479 scopus 로고    scopus 로고
    • Absorption spectroscopy in studies of visual pigments: Spectral and kinetic characterization of intermediates
    • Lewis JW, Kliger DS (2000) Absorption spectroscopy in studies of visual pigments: Spectral and kinetic characterization of intermediates. Methods Enzymol 315:164-178.
    • (2000) Methods Enzymol , vol.315 , pp. 164-178
    • Lewis, J.W.1    Kliger, D.S.2
  • 4
    • 0032412196 scopus 로고    scopus 로고
    • Visual pigment: G-protein-coupled receptor for light signals
    • Shichida Y, Imai H (1998) Visual pigment: G-protein-coupled receptor for light signals. Cell Mol Life Sci 54:1299-1315.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 1299-1315
    • Shichida, Y.1    Imai, H.2
  • 5
    • 34547700719 scopus 로고    scopus 로고
    • 2H NMR of aligned membranes
    • 2H NMR of aligned membranes. J Mol Biol 372:50-66.
    • (2007) J Mol Biol , vol.372 , pp. 50-66
    • Struts, A.V.1
  • 6
    • 33748088543 scopus 로고    scopus 로고
    • 2H NMR structure of retinal in metarhodopsin I
    • 2H NMR structure of retinal in metarhodopsin I. J Am Chem Soc 128:11067-11071.
    • (2006) J Am Chem Soc , vol.128 , pp. 11067-11071
    • Salgado, G.F.1
  • 7
    • 23044486642 scopus 로고    scopus 로고
    • Structure of rhodopsin and the metarhodopsin I photointermediate
    • Schertler GFX (2005) Structure of rhodopsin and the metarhodopsin I photointermediate. Curr Opin Struct Biol 15:408-415.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 408-415
    • Schertler, G.F.X.1
  • 8
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh SP, Zvyaga TA, Lichtarge O, Sakmar TP, Bourne HR (1996) Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383:347-350.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 9
    • 44949236117 scopus 로고    scopus 로고
    • High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • Altenbach C, Kusnetzow AK, Ernst OP, Hofmann KP, Hubbell WL (2008) High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc Natl Acad Sci USA 105:7439-7444.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 10
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens DL, Altenbach C, Yang K, Hubbell WL, Khorana HG (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274:768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 11
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454:183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 12
    • 25144510053 scopus 로고    scopus 로고
    • The role of Glu 181 in the photoactivation of rhodopsin
    • Lüdeke S, et al. (2005) The role of Glu 181 in the photoactivation of rhodopsin. J Mol Biol 353:345-356.
    • (2005) J Mol Biol , vol.353 , pp. 345-356
    • Lüdeke, S.1
  • 13
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the Metarhodopsin II photointermediate of rhodopsin
    • Jäger F, Fahmy K, Sakmar TP, Siebert F (1994) Identification of glutamic acid 113 as the Schiff base proton acceptor in the Metarhodopsin II photointermediate of rhodopsin. Biochemistry 33:10878-10882.
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jäger, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 14
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Arnis S, Fahmy K, Hofmann KP, Sakmar TP (1994) A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J Biol Chem 269:23879-23881.
    • (1994) J Biol Chem , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 15
    • 45649083187 scopus 로고    scopus 로고
    • Functional role of the "ionic lock" - an interhelical hydrogen-bond network in family A heptahelical receptors
    • Vogel R, et al. (2008) Functional role of the "ionic lock" - an interhelical hydrogen-bond network in family A heptahelical receptors. J Mol Biol 380:648-655.
    • (2008) J Mol Biol , vol.380 , pp. 648-655
    • Vogel, R.1
  • 17
    • 0021758996 scopus 로고
    • Temperature and pH dependence of the Metarhodopsin I - Metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions
    • Parkes JH, Liebman PA (1984) Temperature and pH dependence of the Metarhodopsin I - Metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions. Biochemistry 23:5054-5061.
    • (1984) Biochemistry , vol.23 , pp. 5054-5061
    • Parkes, J.H.1    Liebman, P.A.2
  • 18
    • 0027317273 scopus 로고
    • Two different forms of Metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
    • Arnis S, Hofmann KP (1993) Two different forms of Metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc Natl Acad Sci USA 90:7849-7853.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7849-7853
    • Arnis, S.1    Hofmann, K.P.2
  • 20
    • 0027757062 scopus 로고
    • Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II
    • Thorgeirsson TE, Lewis JW, Wallace-Williams SE, Kliger DS (1993) Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II. Biochemistry 32:13861-13872.
    • (1993) Biochemistry , vol.32 , pp. 13861-13872
    • Thorgeirsson, T.E.1    Lewis, J.W.2    Wallace-Williams, S.E.3    Kliger, D.S.4
  • 21
    • 33747625451 scopus 로고    scopus 로고
    • a of the retinal Schiff base
    • a of the retinal Schiff base. J Am Chem Soc 128:10503-10512.
    • (2006) J Am Chem Soc , vol.128 , pp. 10503-10512
    • Vogel, R.1
  • 22
    • 34247228082 scopus 로고    scopus 로고
    • Coupling of protonation switches during rhodopsin activation
    • Vogel R, Sakmar TP, Sheves M, Siebert F (2006) Coupling of protonation switches during rhodopsin activation. Photochem Photobiol 83:286-292.
    • (2006) Photochem Photobiol , vol.83 , pp. 286-292
    • Vogel, R.1    Sakmar, T.P.2    Sheves, M.3    Siebert, F.4
  • 23
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, et al. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 24
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada T, et al. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J Mol Biol 342:571-583.
    • (2004) J Mol Biol , vol.342 , pp. 571-583
    • Okada, T.1
  • 26
    • 0027374544 scopus 로고
    • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and Metarhodopsin II: A Fourier-transform infrared spectroscopy study of site-directed mutants
    • Fahmy K, et al. (1993) Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and Metarhodopsin II: A Fourier-transform infrared spectroscopy study of site-directed mutants. Proc Natl Acad Sci USA 90:10206-10210.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10206-10210
    • Fahmy, K.1
  • 27
    • 24344507257 scopus 로고    scopus 로고
    • Vogel R, Siebert F, Lüdeke S, Hirshfeld A, Sheves M (2005) Agonists and partial agonists of rhodopsin: Retinals with ring modifications. Biochemistry 44:11684-11699, and erratum (2005) 44:12914.
    • Vogel R, Siebert F, Lüdeke S, Hirshfeld A, Sheves M (2005) Agonists and partial agonists of rhodopsin: Retinals with ring modifications. Biochemistry 44:11684-11699, and erratum (2005) 44:12914.
  • 28
    • 32344443931 scopus 로고    scopus 로고
    • Agonists and partial agonists of rhodopsin: Retinal polyene methylation affects receptor activation
    • Vogel R, et al. (2006) Agonists and partial agonists of rhodopsin: Retinal polyene methylation affects receptor activation. Biochemistry 45:1640-1652.
    • (2006) Biochemistry , vol.45 , pp. 1640-1652
    • Vogel, R.1
  • 29
    • 0037014696 scopus 로고    scopus 로고
    • Electrostatic properties of membrane lipids coupled to metarhodopsin II formation in visual transduction
    • Wang Y, Botelho AV, Martinez GV, Brown MF (2002) Electrostatic properties of membrane lipids coupled to metarhodopsin II formation in visual transduction. J Am Chem Soc 124:7690-7701.
    • (2002) J Am Chem Soc , vol.124 , pp. 7690-7701
    • Wang, Y.1    Botelho, A.V.2    Martinez, G.V.3    Brown, M.F.4
  • 30
    • 0027518957 scopus 로고
    • Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes
    • Gibson NJ, Brown MF (1993) Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes. Biochemistry 32:2438-2454.
    • (1993) Biochemistry , vol.32 , pp. 2438-2454
    • Gibson, N.J.1    Brown, M.F.2
  • 31
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • Botelho AV, Huber T, Sakmar TP, Brown MF (2006) Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes. Biophys J 91:4464-4477.
    • (2006) Biophys J , vol.91 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 32
    • 0040141552 scopus 로고    scopus 로고
    • Signaling states of rhodopsin: Retinal provides a scaffold for activating proton transfer switches
    • Meyer CK, et al. (2000) Signaling states of rhodopsin: Retinal provides a scaffold for activating proton transfer switches. J Biol Chem 275:19713-19718.
    • (2000) J Biol Chem , vol.275 , pp. 19713-19718
    • Meyer, C.K.1
  • 33
    • 33947356279 scopus 로고    scopus 로고
    • G protein coupled receptor structure and activation
    • Kobilka BK (2007) G protein coupled receptor structure and activation. Biochim Biophys Acta 1768:794-807.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 794-807
    • Kobilka, B.K.1
  • 34
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of thehumanbeta-2 adrenergic G-protein-coupled receptor
    • Rasmussen SG, et al. (2007) Crystal structure of thehumanbeta-2 adrenergic G-protein-coupled receptor. Nature 450:383-387.
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1
  • 35
    • 47949129742 scopus 로고    scopus 로고
    • 1- adrenergic G-protein-coupled receptor
    • 1- adrenergic G-protein-coupled receptor. Nature 454:486-491.
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 36
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor
    • Cherezov V, et al. (2007) High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318:1258-1265.
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 37
    • 4344674667 scopus 로고    scopus 로고
    • Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge
    • Kim JM, et al. (2004) Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge. Proc Natl Acad Sci USA 101:12508-12513.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12508-12513
    • Kim, J.M.1
  • 38
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy K, Sakmar TP (1993) Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32:7229-7236.
    • (1993) Biochemistry , vol.32 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 39
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus
    • Janz JM, Farrens DL (2004) Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus. J Biol Chem 279:29767-29773.
    • (2004) J Biol Chem , vol.279 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 40
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster DS (1982) Preparation of retinal rod outer segments. Methods Enzymol 81:48-52.
    • (1982) Methods Enzymol , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 41
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by nonlamellar-forming lipids
    • Botelho AV, Gibson NJ, Thurmond RL, Wang Y, Brown MF (2002) Conformational energetics of rhodopsin modulated by nonlamellar-forming lipids. Biochemistry 41:6354-6368.
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Botelho, A.V.1    Gibson, N.J.2    Thurmond, R.L.3    Wang, Y.4    Brown, M.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.