메뉴 건너뛰기




Volumn 43, Issue 29, 2004, Pages 9457-9466

Formation of Meta III during the decay of activated rhodopsin proceeds via Meta I and not via Meta II

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CONFORMATIONS; ISOMERIZATION;

EID: 3242687856     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049337u     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: Structural basis of molecular physiology
    • Menon, S. T., Han, M., and Sakmar, T. P. (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
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: What does the rhodopsin structure tell us?
    • Meng, E. C., and Bourne, H. R. (2001) Receptor activation: what does the rhodopsin structure tell us?, Trends Pharmacol. Sci. 22, 587-593.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 5
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada, T., Ernst, O. P., Palczewski, K., and Hofmann, K. P. (2001) Activation of rhodopsin: new insights from structural and biochemical studies, Trends Biochem. Sci. 26, 318-324.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 6
    • 0037729260 scopus 로고    scopus 로고
    • New insights from FTIR spectroscopy into molecular properties and activation mechanisms of the visual pigment rhodopsin
    • Vogel, R., and Siebert, F. (2003) New insights from FTIR spectroscopy into molecular properties and activation mechanisms of the visual pigment rhodopsin, Biospectroscopy 72, 133-148.
    • (2003) Biospectroscopy , vol.72 , pp. 133-148
    • Vogel, R.1    Siebert, F.2
  • 8
    • 0022869897 scopus 로고
    • Photoproducts of rhodopsin in the disc membrane
    • Hofmann, K. P. (1986) Photoproducts of rhodopsin in the disc membrane, Photobiochem. Photobiophys. 13, 309-327.
    • (1986) Photobiochem. Photobiophys. , vol.13 , pp. 309-327
    • Hofmann, K.P.1
  • 9
    • 0035914463 scopus 로고    scopus 로고
    • Conformations of the active and inactive states of opsin
    • Vogel, R., and Siebert, F. (2001) Conformations of the active and inactive states of opsin, J. Biol. Chem. 276, 38487-38493.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38487-38493
    • Vogel, R.1    Siebert, F.2
  • 10
    • 0023110336 scopus 로고
    • Evidence for rhodopsin refolding during the decay of Meta II
    • Rothschild, K. J., Gillespie, J., and DeGrip, W. J. (1987) Evidence for rhodopsin refolding during the decay of Meta II, Biophys. J. 51, 345-350.
    • (1987) Biophys. J. , vol.51 , pp. 345-350
    • Rothschild, K.J.1    Gillespie, J.2    DeGrip, W.J.3
  • 11
    • 0042473251 scopus 로고    scopus 로고
    • Deactivation of rhodopsin in the transition from the signaling state Meta II to Meta III involves a thermal isomerization of the retinal chromophore C=N double bond
    • Vogel, R., Siebert, F., Mathias, G., Tavan, P., Fan, G. B., and Sheves, M. (2003) Deactivation of rhodopsin in the transition from the signaling state Meta II to Meta III involves a thermal isomerization of the retinal chromophore C=N double bond, Biochemistry 42, 9863-9874.
    • (2003) Biochemistry , vol.42 , pp. 9863-9874
    • Vogel, R.1    Siebert, F.2    Mathias, G.3    Tavan, P.4    Fan, G.B.5    Sheves, M.6
  • 12
    • 0031017636 scopus 로고    scopus 로고
    • Metarhodopsin III formation and decay kinetics: Comparison of bovine and human rhodopsin
    • Lewis, J. W., van Kuijk, F. J., Carruthers, J. A., and Kliger, D. S. (1997) Metarhodopsin III formation and decay kinetics: comparison of bovine and human rhodopsin, Vision Res. 37, 1-8.
    • (1997) Vision Res. , vol.37 , pp. 1-8
    • Lewis, J.W.1    Van Kuijk, F.J.2    Carruthers, J.A.3    Kliger, D.S.4
  • 13
    • 0038729667 scopus 로고    scopus 로고
    • Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II
    • Heck, M., Schädel, S. A., Maretzki, D., Bartl, F. J., Ritter, E., Palczewski, K., and Hofmann, K. P. (2003) Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II, J. Biol. Chem. 278, 3162-3169.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3162-3169
    • Heck, M.1    Schädel, S.A.2    Maretzki, D.3    Bartl, F.J.4    Ritter, E.5    Palczewski, K.6    Hofmann, K.P.7
  • 15
    • 0018320164 scopus 로고
    • The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states and the reversibility of the Meta II-Meta III transition
    • Chabre, M., and Breton, J. (1979) The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states and the reversibility of the Meta II-Meta III transition, Vision Res. 19, 1005-1018.
    • (1979) Vision Res. , vol.19 , pp. 1005-1018
    • Chabre, M.1    Breton, J.2
  • 16
    • 0025823575 scopus 로고
    • Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin
    • Kibelbek, J., Mitchell, D. C., Beach, J. M., and Litman, B. J. (1991) Functional equivalence of metarhodopsin II and the Gt-activating form of photolyzed bovine rhodopsin, Biochemistry 30, 6761-6768.
    • (1991) Biochemistry , vol.30 , pp. 6761-6768
    • Kibelbek, J.1    Mitchell, D.C.2    Beach, J.M.3    Litman, B.J.4
  • 17
    • 37049228254 scopus 로고
    • The light reaction in the bleaching of rhodopsin
    • Wald, G., Durell, J., and St. George, R. C. C. (1950) The light reaction in the bleaching of rhodopsin, Science 111, 179-181.
    • (1950) Science , vol.111 , pp. 179-181
    • Wald, G.1    Durell, J.2    St. George, R.C.C.3
  • 18
    • 0029566281 scopus 로고
    • Structural changes in the lumirhodopsin-to-metarhodopsin I conversion of air-dried bovine rhodopsin
    • Nishimura, S., Sasaki, J., Kandori, H., Lugtenburg, J., and Maeda, A. (1995) Structural changes in the lumirhodopsin-to-metarhodopsin I conversion of air-dried bovine rhodopsin, Biochemistry 34, 16758-16763.
    • (1995) Biochemistry , vol.34 , pp. 16758-16763
    • Nishimura, S.1    Sasaki, J.2    Kandori, H.3    Lugtenburg, J.4    Maeda, A.5
  • 19
    • 0021882555 scopus 로고
    • Effects of lipid environment on the light-induced conformational changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state
    • Baldwin, P. A., and Hubbell, W. L. (1985) Effects of lipid environment on the light-induced conformational changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state, Biochemistry 24, 2633-2639.
    • (1985) Biochemistry , vol.24 , pp. 2633-2639
    • Baldwin, P.A.1    Hubbell, W.L.2
  • 21
    • 0027518957 scopus 로고
    • Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes
    • Gibson, N. J., and Brown, M. F. (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
  • 22
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster, D. S. (1982) Preparation of retinal rod outer segments, Methods Enzymol. 81, 48-52.
    • (1982) Methods Enzymol. , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 23
    • 0020007210 scopus 로고
    • Purification of bovine rhodopsin over cancanavalin A-Sepharose
    • DeGrip, W. J. (1982) Purification of bovine rhodopsin over cancanavalin A-Sepharose, Methods Enzymol. 81, 197-207.
    • (1982) Methods Enzymol. , vol.81 , pp. 197-207
    • DeGrip, W.J.1
  • 24
    • 0018901497 scopus 로고
    • Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes
    • Kühn, H. (1980) Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes, Nature 283, 587-589.
    • (1980) Nature , vol.283 , pp. 587-589
    • Kühn, H.1
  • 25
    • 0000519923 scopus 로고
    • Flow of information in the light-triggered cyclic nucleotide cascade of vision
    • Fung, B. K. K., Hurley, J. B., and Stryer, L. (1981) Flow of information in the light-triggered cyclic nucleotide cascade of vision, Proc. Natl. Acad. Sci. U.S.A. 78, 152-156.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 152-156
    • Fung, B.K.K.1    Hurley, J.B.2    Stryer, L.3
  • 26
    • 0023708657 scopus 로고
    • The intrinsic fluorescence of the alpha subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange
    • Phillips, W. J., and Cerione, R. A. (1988) The intrinsic fluorescence of the alpha subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange, J. Biol. Chem. 263, 15498-15505.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15498-15505
    • Phillips, W.J.1    Cerione, R.A.2
  • 28
    • 0001269731 scopus 로고
    • Apparent molar hear capacities of phospholipids in aqueous dispersion. Effects of chain length and headgroup structure
    • Blume, A. (1983) Apparent molar hear capacities of phospholipids in aqueous dispersion. Effects of chain length and headgroup structure, Biochemistry 22, 5436-5442.
    • (1983) Biochemistry , vol.22 , pp. 5436-5442
    • Blume, A.1
  • 29
    • 0015737614 scopus 로고
    • Temperature- and light-dependent structural changes in rhodopsin-lipid membranes
    • Chen, Y. S., and Hubbell, W. L. (1973) Temperature- and light-dependent structural changes in rhodopsin-lipid membranes, Exp. Eye Res. 17, 517-532.
    • (1973) Exp. Eye Res. , vol.17 , pp. 517-532
    • Chen, Y.S.1    Hubbell, W.L.2
  • 30
    • 0030043913 scopus 로고    scopus 로고
    • Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library
    • Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996) Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library, J. Biol. Chem. 271, 361-366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 361-366
    • Martin, E.L.1    Rens-Domiano, S.2    Schatz, P.J.3    Hamm, H.E.4
  • 31
    • 0037133546 scopus 로고    scopus 로고
    • Conformation and stability of α-helical membrane proteins. 2. Influence of pH and salts on stability and unfolding of rhodopsin
    • Vogel, R., and Siebert, F. (2002) Conformation and stability of α-helical membrane proteins. 2. Influence of pH and salts on stability and unfolding of rhodopsin, Biochemistry 41, 3536-3545.
    • (2002) Biochemistry , vol.41 , pp. 3536-3545
    • Vogel, R.1    Siebert, F.2
  • 32
    • 0035895353 scopus 로고    scopus 로고
    • Salt dependence of the formation and stability of the signaling state in G protein-coupled receptors: Evidence for the involvement of the Hofmeister effect
    • Vogel, R., Fan, G. B., Sheves, M., and Siebert, F. (2001) Salt dependence of the formation and stability of the signaling state in G protein-coupled receptors: evidence for the involvement of the Hofmeister effect, Biochemistry 40, 483-493.
    • (2001) Biochemistry , vol.40 , pp. 483-493
    • Vogel, R.1    Fan, G.B.2    Sheves, M.3    Siebert, F.4
  • 33
    • 0034671530 scopus 로고    scopus 로고
    • Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains
    • Abdulaev, N. G., Ngo, T., Chen, R., Lu, Z., and Ridge, K. D. (2000) Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains, J. Biol. Chem. 275, 39354-39363.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39354-39363
    • Abdulaev, N.G.1    Ngo, T.2    Chen, R.3    Lu, Z.4    Ridge, K.D.5
  • 34
    • 0035839574 scopus 로고    scopus 로고
    • Signaling states of rhodopsin: Absorption of light in active Metarhodopsin II generates an all-trans-retinal bound inactive state
    • Bartl, F. J., Ritter, E., and Hofmann, K. P. (2001) Signaling states of rhodopsin: absorption of light in active Metarhodopsin II generates an all-trans-retinal bound inactive state, J. Biol. Chem. 276, 30161-30166.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30161-30166
    • Bartl, F.J.1    Ritter, E.2    Hofmann, K.P.3
  • 35
    • 0018867251 scopus 로고
    • Incorporation of photoreceptor membrane into a multilamellar film
    • Rothschild, K. J., Rosen, K. M., and Clark, N. A. (1980) Incorporation of photoreceptor membrane into a multilamellar film, Biophys. J. 31, 45-52.
    • (1980) Biophys. J. , vol.31 , pp. 45-52
    • Rothschild, K.J.1    Rosen, K.M.2    Clark, N.A.3
  • 36
    • 0032546596 scopus 로고    scopus 로고
    • Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin
    • Beck, M., Sakmar, T. P., and Siebert, F. (1998) Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin, Biochemistry 37, 7630-7639.
    • (1998) Biochemistry , vol.37 , pp. 7630-7639
    • Beck, M.1    Sakmar, T.P.2    Siebert, F.3
  • 37
    • 0019532559 scopus 로고
    • The involvement of water at the retinal binding site in rhodopsin and early light-induced intramolecular proton transfer
    • Rafferty, C. N., and Shichi, H. (1981) The involvement of water at the retinal binding site in rhodopsin and early light-induced intramolecular proton transfer, Photochem. Photobiol. 33, 229-234.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 229-234
    • Rafferty, C.N.1    Shichi, H.2
  • 38
    • 0024200660 scopus 로고
    • The photoreaction of vacuum-dried rhodopsin at low temperature: Evidence for charge stabilization by water
    • Ganter, U. M., Schmid, E. D., and Siebert, F. (1988) The photoreaction of vacuum-dried rhodopsin at low temperature: evidence for charge stabilization by water, J. Photochem. Photobiol. B 2, 417-426.
    • (1988) J. Photochem. Photobiol. B , vol.2 , pp. 417-426
    • Ganter, U.M.1    Schmid, E.D.2    Siebert, F.3
  • 40
    • 0001773626 scopus 로고
    • Effects of dehydration on membranes and membrane stabilization at low water activities
    • (Chapman, D., Ed.), Academic Press, London
    • Crowe, J. C., and Crowe, L. M. (1984) Effects of dehydration on membranes and membrane stabilization at low water activities, in Biological Membranes (Chapman, D., Ed.) pp 57-103, Academic Press, London.
    • (1984) Biological Membranes , pp. 57-103
    • Crowe, J.C.1    Crowe, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.