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Volumn 796, Issue , 2012, Pages 133-174

Allosteric mechanisms of G protein-coupled receptor signaling: A structural perspective

Author keywords

G protein coupled receptor; Heterotrimeric G proteins; Receptor mediated nucleotide exchange; Rhodopsin; Transducin

Indexed keywords

G PROTEIN COUPLED RECEPTOR; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; RHODOPSIN; TRANSDUCIN;

EID: 82455179081     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-334-9_8     Document Type: Article
Times cited : (13)

References (57)
  • 2
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • DOI 10.1038/nature07063, PII NATURE07063
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin, Nature 454, 183-187. (Pubitemid 351969893)
    • (2008) Nature , vol.454 , Issue.7201 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.-W.4    Ernst, O.P.5
  • 3
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit
    • Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B., and Hofmann, K. P. (1988) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit, Science 241, 832-835.
    • (1988) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1    Deretic, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5    Hofmann, K.P.6
  • 4
    • 0027132717 scopus 로고
    • The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
    • Noel, J. P., Hamm, H. E., and Sigler, P. B. (1993) The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S, Nature 366, 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 5
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 angstrom crystal structure of a heterotrimeric G protein
    • Lambright, D. G., Sondek, J., Bohm, A., Skiba, N. P., Hamm, H. E., and Sigler, P. B. (1996) The 2.0 angstrom crystal structure of a heterotrimeric G protein, Nature 379, 311-319.
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1    Sondek, J.2    Bohm, A.3    Skiba, N.P.4    Hamm, H.E.5    Sigler, P.B.6
  • 6
    • 0028027596 scopus 로고
    • GTPase mechanism of Gproteins from the 1.7-Angstroms crystal structure of transducin alpha.GDP.AIF4
    • DOI 10.1038/372276a0
    • Sondek, J., Lambright, D. G., Noel, J. P., Hamm, H. E., and Sigler, P. B. (1994) GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4, Nature 372, 276-279. (Pubitemid 2152279)
    • (1994) Nature , vol.372 , Issue.6503 , pp. 276-279
    • Sondek, J.1    Lambright, D.G.2    Noel, J.P.3    Hamm, H.E.4    Sigler, P.B.5
  • 8
    • 73549104285 scopus 로고    scopus 로고
    • The year in G protein-coupled receptor research
    • Millar, R. P., and Newton, C. L. (2010) The year in G protein-coupled receptor research, Mol Endocrinol 24, 261-274.
    • (2010) Mol Endocrinol , vol.24 , pp. 261-274
    • Millar, R.P.1    Newton, C.L.2
  • 10
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • DOI 10.1038/362770a0
    • Schertler, G. F., Villa, C., and Henderson, R. (1993) Projection structure of rhodopsin, Nature 362, 770-772. (Pubitemid 23125985)
    • (1993) Nature , vol.362 , Issue.6422 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 12
    • 0024110575 scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
    • Karnik, S. S., Sakmar, T. P., Chen, H. B., and Khorana, H. G. (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin, Proc Natl Acad Sci U S A 85, 8459-8463.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8459-8463
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.B.3    Khorana, H.G.4
  • 13
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros, J. A., Jensen, A. D., Liapakis, G., Rasmussen, S. G., Shi, L., Gether, U., and Javitch, J. A. (2001) Activation of the beta 2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6, J Biol Chem 276, 29171-29177.
    • (2001) J Biol Chem , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 14
    • 0037174606 scopus 로고    scopus 로고
    • β2 adrenergic receptor activation: Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • DOI 10.1074/jbc.M206801200
    • Shi, L., Liapakis, G., Xu, R., Guarnieri, F., Ballesteros, J. A., and Javitch, J. A. (2002) Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch, J Biol Chem 277, 40989-40996. (Pubitemid 35215688)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 15
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • DOI 10.1021/bi027224+
    • Mirzadegan, T., Benko, G., Filipek, S., and Palczewski, K. (2003) Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin, Biochemistry 42, 2759-2767. (Pubitemid 36331518)
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 16
    • 0016253492 scopus 로고
    • Rhodopsin content in the outer segment membranes of bovine and frog retinal rods
    • Papermaster, D. S., and Dreyer, W. J. (1974) Rhodopsin content in the outer segment membranes of bovine and frog retinal rods, Biochemistry 13, 2438-2444.
    • (1974) Biochemistry , vol.13 , pp. 2438-2444
    • Papermaster, D.S.1    Dreyer, W.J.2
  • 20
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • DOI 10.1038/nature06925, PII NATURE06925
    • Murakami, M., and Kouyama, T. (2008) Crystal structure of squid rhodopsin, Nature 453, 363-367. (Pubitemid 351693128)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 23
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Unger, V. M., and Schertler, G. F. (1995) Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy, Biophys J 68, 1776-1786.
    • (1995) Biophys J , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.2
  • 24
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • DOI 10.1126/science.274.5288.768
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., and Khorana, H. G. (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin, Science 274, 768-770. (Pubitemid 26398253)
    • (1996) Science , vol.274 , Issue.5288 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 27
    • 0023062991 scopus 로고
    • G-proteins - Transducers of receptor-generated signals
    • Gilman, A. G. (1987) G-Proteins - Transducers of Receptor-Generated Signals, Annual Review of Biochemistry 56, 615-649.
    • (1987) Annual Review of Biochemistry , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 28
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • DOI 10.1006/geno.1999.5992
    • Downes, G. B., and Gautam, N. (1999) The G protein subunit gene families, Genomics 62, 544-552. (Pubitemid 30075189)
    • (1999) Genomics , vol.62 , Issue.3 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 30
    • 2642689663 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domains of adenylyl cyclase in a complex with G(sα)·GTPγΣ
    • DOI 10.1126/science.278.5345.1907
    • Tesmer, J. J., Sunahara, R. K., Gilman, A. G., and Sprang, S. R. (1997) Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS, Science 278, 1907-1916. (Pubitemid 28013225)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1907-1916
    • Tesmer, J.J.G.1    Sunahara, R.K.2    Gilman, A.G.3    Sprang, S.R.4
  • 31
    • 0027965652 scopus 로고
    • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
    • Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M. E., Gilman, A. G., and Sprang, S. R. (1994) Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis, Science 265, 1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 32
    • 0028862026 scopus 로고
    • Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis
    • Mixon, M. B., Lee, E., Coleman, D. E., Berghuis, A. M., Gilman, A. G., and Sprang, S. R. (1995) Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis, Science 270, 954-960.
    • (1995) Science , vol.270 , pp. 954-960
    • Mixon, M.B.1    Lee, E.2    Coleman, D.E.3    Berghuis, A.M.4    Gilman, A.G.5    Sprang, S.R.6
  • 34
    • 0032514722 scopus 로고    scopus 로고
    • 2+: A crystallographic titration experiment
    • DOI 10.1021/bi9810306
    • Coleman, D. E., and Sprang, S. R. (1998) Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2p: a crystallographic titration experiment, Biochemistry 37, 14376-14385. (Pubitemid 28489043)
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14376-14385
    • Coleman, D.E.1    Sprang, S.R.2
  • 35
    • 0026774642 scopus 로고
    • Promotion of the GTP-liganded state of the Go alpha protein by deletion of the C terminus
    • Denker, B. M., Schmidt, C. J., and Neer, E. J. (1992) Promotion of the GTP-liganded state of the Go alpha protein by deletion of the C terminus, J Biol Chem 267, 9998-10002.
    • (1992) J Biol Chem , vol.267 , pp. 9998-10002
    • Denker, B.M.1    Schmidt, C.J.2    Neer, E.J.3
  • 36
    • 0028988578 scopus 로고
    • Interactions between the amino- and carboxyl-terminal regions of G alpha subunits: Analysis of mutated G alpha o/G alpha i2 chimeras
    • Denker, B. M., Boutin, P. M., and Neer, E. J. (1995) Interactions between the amino- and carboxyl-terminal regions of G alpha subunits: analysis of mutated G alpha o/G alpha i2 chimeras, Biochemistry 34, 5544-5553.
    • (1995) Biochemistry , vol.34 , pp. 5544-5553
    • Denker, B.M.1    Boutin, P.M.2    Neer, E.J.3
  • 37
    • 0034098381 scopus 로고    scopus 로고
    • A surface-exposed region of G(sα) in which substitutions decrease receptor-mediated activation and increase receptor affinity
    • Grishina, G., and Berlot, C. H. (2000) A surface- exposed region of G(salpha) in which substitutions decrease receptor-mediated activation and increase receptor affinity, Mol Pharmacol 57, 1081-1092. (Pubitemid 30354380)
    • (2000) Molecular Pharmacology , vol.57 , Issue.6 , pp. 1081-1092
    • Grishina, G.1    Berlot, C.H.2
  • 38
    • 52949153619 scopus 로고    scopus 로고
    • Receptor-mediated changes at the myristoylated amino terminus of Galpha(il) proteins
    • Preininger, A. M., Parello, J., Meier, S. M., Liao, G., and Hamm, H. E. (2008) Receptor-mediated changes at the myristoylated amino terminus of Galpha(il) proteins, Biochemistry 47, 10281-10293.
    • (2008) Biochemistry , vol.47 , pp. 10281-10293
    • Preininger, A.M.1    Parello, J.2    Meier, S.M.3    Liao, G.4    Hamm, H.E.5
  • 39
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling
    • Kisselev, O. G., Ermolaeva, M. V., and Gautam, N. (1994) A farnesylated domain in the G protein gamma subunit is a specific determinant of receptor coupling, J Biol Chem 269, 21399-21402. (Pubitemid 24274763)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.34 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 40
    • 0030043913 scopus 로고    scopus 로고
    • Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library
    • DOI 10.1074/jbc.271.1.361
    • 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. (Pubitemid 26026603)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 361-366
    • Martin, E.L.1    Rens-Domiano, S.2    Schatz, P.J.3    Hamm, H.E.4
  • 41
    • 0028101036 scopus 로고
    • Synthetic peptides as probes for G protein function. Carboxyl-terminal G alpha s peptides mimic Gs and evoke high affinity agonist binding to beta-adrenergic receptors
    • Rasenick, M. M.,Watanabe, M., Lazarevic, M. B., Hatta, S., and Hamm, H. E. (1994) Synthetic peptides as probes for G protein function. Carboxyl-terminal G alpha s peptides mimic Gs and evoke high affinity agonist binding to beta-adrenergic receptors, J Biol Chem 269, 21519-21525.
    • (1994) J Biol Chem , vol.269 , pp. 21519-21525
    • Rasenick, M.1    Watanabe, M.M.2    Lazarevic, M.B.3    Hatta, S.4    Hamm, H.E.5
  • 42
    • 0028172426 scopus 로고
    • Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha
    • Taylor, J. M., Jacob-Mosier, G. G., Lawton, R. G., Remmers, A. E., and Neubig, R. R. (1994) Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha, J Biol Chem 269, 27618-27624.
    • (1994) J Biol Chem , vol.269 , pp. 27618-27624
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Remmers, A.E.4    Neubig, R.R.5
  • 43
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gbeta. A receptor-derived peptide binds to the carboxyl terminus
    • Taylor, J. M., Jacob-Mosier, G. G., Lawton, R. G., VanDort, M., and Neubig, R. R. (1996) Receptor and membrane interaction sites on Gbeta. A receptor-derived peptide binds to the carboxyl terminus, J Biol Chem 271, 3336-3339.
    • (1996) J Biol Chem , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Vandort, M.4    Neubig, R.R.5
  • 44
    • 0035942229 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent
    • DOI 10.1073/pnas.051632998
    • Itoh, Y., Cai, K., and Khorana, H. G. (2001) Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent, Proc Natl Acad Sci U S A 98, 4883-4887. (Pubitemid 32397051)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 45
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • DOI 10.1073/pnas.051632898
    • Cai, K., Itoh, Y., and Khorana, H. G. (2001) Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent, Proc Natl Acad Sci U S A 98, 4877-4882. (Pubitemid 32397050)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 46
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex
    • Lichtarge, O., Bourne, H. R., and Cohen, F. E. (1996) Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex, Proc Natl Acad Sci U S A 93, 7507-7511.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 47
    • 0030614427 scopus 로고    scopus 로고
    • Receptor and βγ binding sites in the α subunit of the retinal G protein transducin
    • DOI 10.1126/science.275.5298.381
    • Onrust, R., Herzmark, P., Chi, P., Garcia, P. D., Lichtarge, O., Kingsley, C., and Bourne, H. R. (1997) Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin, Science 275, 381-384. (Pubitemid 27051613)
    • (1997) Science , vol.275 , Issue.5298 , pp. 381-384
    • Onrust, R.1    Herzmark, P.2    Chi, P.3    Garcia, P.D.4    Lichtarge, O.5    Kingsley, C.6    Bourne, H.R.7
  • 48
    • 0037018839 scopus 로고    scopus 로고
    • Disruption of the α5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange
    • DOI 10.1021/bi025514k
    • Marin, E. P., Krishna, A. G., and Sakmar, T. P. (2002) Disruption of the alpha5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange, Biochemistry 41, 6988-6994. (Pubitemid 34575670)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 6988-6994
    • Marin, E.P.1    Krishna, A.G.2    Sakmar, T.P.3
  • 50
    • 0037221946 scopus 로고    scopus 로고
    • Activation of G-protein Gα subunits by receptors through Gα-Gβ and Gα-Gγ interactions
    • DOI 10.1016/S0968-0004(02)00006-3, PII S0968000402000063
    • Cherfils, J., and Chabre, M. (2003) Activation of G-protein G alpha subunits by receptors through G alpha-G beta and G alpha-G gamma interactions, Trends in Biochemical Sciences 28, 13-17. (Pubitemid 36051001)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 13-17
    • Cherfils, J.1    Chabre, M.2
  • 51
    • 33747739191 scopus 로고    scopus 로고
    • Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors
    • DOI 10.1074/jbc.M602277200
    • Rondard, P., Liu, J., Huang, S., Malhaire, F., Vol, C., Pinault, A., Labesse, G., and Pin, J. P. (2006) Coupling of agonist binding to effector domain activation in metabotropic glutamate-like receptors, J Biol Chem 281, 24653-24661. (Pubitemid 44274238)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24653-24661
    • Rondard, P.1    Liu, J.2    Huang, S.3    Malhaire, F.4    Vol, C.5    Pinault, A.6    Labesse, G.7    Pin, J.-P.8
  • 54
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • DOI 10.1016/j.jmb.2004.07.044, PII S0022283604008733
    • Okada,T., Sugihara, M.,Bondar, A.N.,Elstner, M., Entel, P., and Buss, V. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure, J Mol Biol 342, 571-583. (Pubitemid 39149759)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.-N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 56
    • 0018130363 scopus 로고
    • Inactivation of the protease inhibitor phenylmethylsulfonyl fluoride in buffers
    • James, G. T. (1978) Inactivation of the protease inhibitor phenylmethylsulfonyl fluoride in buffers, Anal Biochem 86, 574-579. (Pubitemid 9059104)
    • (1978) Analytical Biochemistry , vol.86 , Issue.2 , pp. 574-579
    • James, G.T.1


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