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Volumn 74, Issue , 2007, Pages 67-93

How do Receptors Activate G Proteins?

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; RECEPTOR;

EID: 34548439826     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(07)74002-0     Document Type: Review
Times cited : (55)

References (126)
  • 1
    • 0035951805 scopus 로고    scopus 로고
    • Structural requirements for the stabilization of metarhodopsin II by the C terminus of the α subunit of transducin
    • Aris L., Gilchrist A., Rens-Domiano S., Meyer C., Schatz P.J., Dratz E.A., and Hamm H.E. Structural requirements for the stabilization of metarhodopsin II by the C terminus of the α subunit of transducin. J. Biol. Chem. 276 (2001) 2333-2339
    • (2001) J. Biol. Chem. , vol.276 , pp. 2333-2339
    • Aris, L.1    Gilchrist, A.2    Rens-Domiano, S.3    Meyer, C.4    Schatz, P.J.5    Dratz, E.A.6    Hamm, H.E.7
  • 2
    • 0035834710 scopus 로고    scopus 로고
    • G protein γ subunit interaction with a receptor regulates receptor-stimulated nucleotide exchange
    • Azpiazu I., and Gautam N. G protein γ subunit interaction with a receptor regulates receptor-stimulated nucleotide exchange. J. Biol. Chem. 276 (2001) 41742-41747
    • (2001) J. Biol. Chem. , vol.276 , pp. 41742-41747
    • Azpiazu, I.1    Gautam, N.2
  • 3
    • 0033544847 scopus 로고    scopus 로고
    • A G protein γ subunit-specific peptide inhibits muscarinic receptor signaling
    • Azpiazu I., Cruzblanca H., Li P., Linder M., Zhuo M., and Gautam N. A G protein γ subunit-specific peptide inhibits muscarinic receptor signaling. J. Biol. Chem. 274 (1999) 35305-35308
    • (1999) J. Biol. Chem. , vol.274 , pp. 35305-35308
    • Azpiazu, I.1    Cruzblanca, H.2    Li, P.3    Linder, M.4    Zhuo, M.5    Gautam, N.6
  • 9
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne H.R. How receptors talk to trimeric G proteins. Curr. Opin. Cell Biol. 9 (1997) 134-142
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 12
    • 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
    • Cai K., Itoh Y., and Khorana H.G. 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. USA 98 (2001) 4877-4882
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 13
    • 1842851911 scopus 로고    scopus 로고
    • Molecular dynamics simulations of transducin: Interdomain and front to back communication in activation and nucleotide exchange
    • Ceruso M.A., Periole X., and Weinstein H. Molecular dynamics simulations of transducin: Interdomain and front to back communication in activation and nucleotide exchange. J. Mol. Biol. 338 (2004) 469-481
    • (2004) J. Mol. Biol. , vol.338 , pp. 469-481
    • Ceruso, M.A.1    Periole, X.2    Weinstein, H.3
  • 14
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • Chabre M., and le Maire M. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44 (2005) 9395-9403
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    le Maire, M.2
  • 15
    • 0037221946 scopus 로고    scopus 로고
    • Activation of G-protein Gα subunits by receptors through Gα-Gβ and Gα-Gγ interactions
    • Cherfils J., and Chabre M. Activation of G-protein Gα subunits by receptors through Gα-Gβ and Gα-Gγ interactions. Trends Biochem. Sci. 28 (2003) 13-17
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 13-17
    • Cherfils, J.1    Chabre, M.2
  • 22
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • Downes G.B., and Gautam N. The G protein subunit gene families. Genomics 62 (1999) 544-552
    • (1999) Genomics , vol.62 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 24
    • 0034695482 scopus 로고    scopus 로고
    • Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits
    • Ernst O.P., Meyer C.K., Marin E.P., Henklein P., Fu W.Y., Sakmar T.P., and Hofmann K.P. Mutation of the fourth cytoplasmic loop of rhodopsin affects binding of transducin and peptides derived from the carboxyl-terminal sequences of transducin α and γ subunits. J. Biol. Chem. 275 (2000) 1937-1943
    • (2000) J. Biol. Chem. , vol.275 , pp. 1937-1943
    • Ernst, O.P.1    Meyer, C.K.2    Marin, E.P.3    Henklein, P.4    Fu, W.Y.5    Sakmar, T.P.6    Hofmann, K.P.7
  • 25
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., and Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 (1996) 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
  • 27
    • 0031283166 scopus 로고    scopus 로고
    • 1 adenosine receptors and G proteins in phospholipid vesicles: βγ-subunit composition influences guanine nucleotide exchange and agonist binding
    • 1 adenosine receptors and G proteins in phospholipid vesicles: βγ-subunit composition influences guanine nucleotide exchange and agonist binding. Biochemistry 36 (1997) 16288-16299
    • (1997) Biochemistry , vol.36 , pp. 16288-16299
    • Figler, R.A.1    Lindorfer, M.A.2    Graber, S.G.3    Garrison, J.C.4    Linden, J.5
  • 32
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • Fredriksson R., and Schiöth H.B. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol. Pharmacol. 67 (2005) 1414-1425
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schiöth, H.B.2
  • 33
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 21 (2000) 90-113
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 34
  • 35
    • 0029784196 scopus 로고    scopus 로고
    • The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
    • Gilchrist R.L., Ryu K.S., Ji I., and Ji T.H. The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals. J. Biol. Chem. 271 (1996) 19283-19287
    • (1996) J. Biol. Chem. , vol.271 , pp. 19283-19287
    • Gilchrist, R.L.1    Ryu, K.S.2    Ji, I.3    Ji, T.H.4
  • 36
    • 0032510982 scopus 로고    scopus 로고
    • sα impair receptor-mediated activation by altering receptor and guanine nucleotide binding
    • sα impair receptor-mediated activation by altering receptor and guanine nucleotide binding. J. Biol. Chem. 273 (1998) 15053-15060
    • (1998) J. Biol. Chem. , vol.273 , pp. 15053-15060
    • Grishina, G.1    Berlot, C.H.2
  • 37
    • 0034098381 scopus 로고    scopus 로고
    • sα in which substitutions decrease receptor-mediated activation and increase receptor affinity
    • sα in which substitutions decrease receptor-mediated activation and increase receptor affinity. Mol. Pharmacol. 57 (2000) 1081-1092
    • (2000) Mol. Pharmacol. , vol.57 , pp. 1081-1092
    • Grishina, G.1    Berlot, C.H.2
  • 38
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm H.E. The many faces of G protein signaling. J. Biol. Chem. 273 (1998) 669-672
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 39
    • 0023716027 scopus 로고
    • Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit
    • Hamm H.E., Deretic D., Arendt A., Hargrave P.A., Koenig B., and Hofmann K.P. Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit. Science 241 (1988) 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
  • 40
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: Searching for the structure behind the signal
    • Hedin K.E., Duerson K., and Clapham D.E. Specificity of receptor-G protein interactions: Searching for the structure behind the signal. Cell. Signal. 5 (1993) 505-518
    • (1993) Cell. Signal. , vol.5 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 41
    • 3342875499 scopus 로고    scopus 로고
    • Identification of a novel site within G protein α subunits important for specificity of receptor-G protein interaction
    • Heydorn A., Ward R.J., Jorgensen R., Rosenkilde M.M., Frimurer T.M., Milligan G., and Kostenis E. Identification of a novel site within G protein α subunits important for specificity of receptor-G protein interaction. Mol. Pharmacol. 66 (2004) 250-259
    • (2004) Mol. Pharmacol. , vol.66 , pp. 250-259
    • Heydorn, A.1    Ward, R.J.2    Jorgensen, R.3    Rosenkilde, M.M.4    Frimurer, T.M.5    Milligan, G.6    Kostenis, E.7
  • 44
    • 0033623204 scopus 로고    scopus 로고
    • z is required for receptor recognition, whereas its α4/β6 loop is essential for inhibition of adenylyl cyclase
    • z is required for receptor recognition, whereas its α4/β6 loop is essential for inhibition of adenylyl cyclase. Mol. Pharmacol. 58 (2000) 993-1000
    • (2000) Mol. Pharmacol. , vol.58 , pp. 993-1000
    • Ho, M.K.1    Wong, Y.H.2
  • 45
    • 0034671531 scopus 로고    scopus 로고
    • Selective role of G protein γ subunits in receptor interaction
    • Hou Y., Azpiazu I., Smrcka A., and Gautam N. Selective role of G protein γ subunits in receptor interaction. J. Biol. Chem. 275 (2000) 38961-38964
    • (2000) J. Biol. Chem. , vol.275 , pp. 38961-38964
    • Hou, Y.1    Azpiazu, I.2    Smrcka, A.3    Gautam, N.4
  • 46
    • 0035827658 scopus 로고    scopus 로고
    • G protein β subunit types differentially interact with a muscarinic receptor but not adenylyl cyclase type II or phospholipase C-β2/3
    • Hou Y., Chang V., Capper A.B., Taussig R., and Gautam N. G protein β subunit types differentially interact with a muscarinic receptor but not adenylyl cyclase type II or phospholipase C-β2/3. J. Biol. Chem. 276 (2001) 19982-19988
    • (2001) J. Biol. Chem. , vol.276 , pp. 19982-19988
    • Hou, Y.1    Chang, V.2    Capper, A.B.3    Taussig, R.4    Gautam, N.5
  • 47
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell W.L., Altenbach C., Hubbell C.M., and Khorana H.G. Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Protein Chem. 63 (2003) 243-290
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 49
    • 0032474767 scopus 로고    scopus 로고
    • G-protein diseases furnish a model for the turn-on switch
    • Iiri T., Farfel Z., and Bourne H.R. G-protein diseases furnish a model for the turn-on switch. Nature 394 (1998) 35-38
    • (1998) Nature , vol.394 , pp. 35-38
    • Iiri, T.1    Farfel, Z.2    Bourne, H.R.3
  • 50
    • 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
    • Itoh Y., Cai K., and Khorana H.G. 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. USA 98 (2001) 4883-4887
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 51
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus
    • Janz J.M., and Farrens D.L. Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus. J. Biol. Chem. 279 (2004) 29767-29773
    • (2004) J. Biol. Chem. , vol.279 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 52
    • 6944237210 scopus 로고    scopus 로고
    • The ants go marching two by two: Oligomeric structure of G-protein-coupled receptors
    • Javitch J.A. The ants go marching two by two: Oligomeric structure of G-protein-coupled receptors. Mol. Pharmacol. 66 (2004) 1077-1082
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1077-1082
    • Javitch, J.A.1
  • 54
    • 0035930546 scopus 로고    scopus 로고
    • Gβγ affinity for bovine rhodopsin is determined by the carboxyl-terminal sequences of the γ subunit
    • Jian X., Clark W.A., Kowalak J., Markey S.P., Simonds W.F., and Northup J.K. Gβγ affinity for bovine rhodopsin is determined by the carboxyl-terminal sequences of the γ subunit. J. Biol. Chem. 276 (2001) 48518-48525
    • (2001) J. Biol. Chem. , vol.276 , pp. 48518-48525
    • Jian, X.1    Clark, W.A.2    Kowalak, J.3    Markey, S.P.4    Simonds, W.F.5    Northup, J.K.6
  • 56
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: The promise and the problem
    • Kenakin T. Ligand-selective receptor conformations revisited: The promise and the problem. Trends Pharmacol. Sci. 24 (2003) 346-354
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 57
    • 0027435265 scopus 로고
    • Specific interaction with rhodopsin is dependent on the γ subunit type in a G protein
    • Kisselev O., and Gautam N. Specific interaction with rhodopsin is dependent on the γ subunit type in a G protein. J. Biol. Chem. 268 (1993) 24519-24522
    • (1993) J. Biol. Chem. , vol.268 , pp. 24519-24522
    • Kisselev, O.1    Gautam, N.2
  • 58
    • 0029026880 scopus 로고
    • Receptor-G protein coupling is established by a potential conformational switch in the βγ complex
    • Kisselev O., Pronin A., Ermolaeva M., and Gautam N. Receptor-G protein coupling is established by a potential conformational switch in the βγ complex. Proc. Natl. Acad. Sci. USA 92 (1995) 9102-9106
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9102-9106
    • Kisselev, O.1    Pronin, A.2    Ermolaeva, M.3    Gautam, N.4
  • 59
    • 0037387322 scopus 로고    scopus 로고
    • Rhodopsin controls a conformational switch on the transducin γ subunit
    • Kisselev O.G., and Downs M.A. Rhodopsin controls a conformational switch on the transducin γ subunit. Structure 11 (2003) 367-373
    • (2003) Structure , vol.11 , pp. 367-373
    • Kisselev, O.G.1    Downs, M.A.2
  • 60
    • 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. A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J. Biol. Chem. 269 (1994) 21399-21402
    • (1994) J. Biol. Chem. , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 62
    • 0033609101 scopus 로고    scopus 로고
    • Signal transfer from rhodopsin to the G-protein: Evidence for a two-site sequential fit mechanism
    • Kisselev O.G., Meyer C.K., Heck M., Ernst O.P., and Hofmann K.P. Signal transfer from rhodopsin to the G-protein: Evidence for a two-site sequential fit mechanism. Proc. Natl. Acad. Sci. USA 96 (1999) 4898-4903
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4898-4903
    • Kisselev, O.G.1    Meyer, C.K.2    Heck, M.3    Ernst, O.P.4    Hofmann, K.P.5
  • 63
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • Koenig B.W., Kontaxis G., Mitchell D.C., Louis J.M., Litman B.J., and Bax A. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. J. Mol. Biol. 322 (2002) 441-461
    • (2002) J. Mol. Biol. , vol.322 , pp. 441-461
    • Koenig, B.W.1    Kontaxis, G.2    Mitchell, D.C.3    Louis, J.M.4    Litman, B.J.5    Bax, A.6
  • 67
    • 0032504227 scopus 로고    scopus 로고
    • q subunits displaying promiscuous receptor coupling properties
    • q subunits displaying promiscuous receptor coupling properties. J. Biol. Chem. 273 (1998) 17886-17892
    • (1998) J. Biol. Chem. , vol.273 , pp. 17886-17892
    • Kostenis, E.1    Zeng, F.Y.2    Wess, J.3
  • 69
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K. Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103 (2004) 21-80
    • (2004) Pharmacol. Ther. , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 70
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright D.G., Noel J.P., Hamm H.E., and Sigler P.B. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369 (1994) 621-628
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 72
    • 0029106731 scopus 로고
    • α16 contribute to the specificity of activation by the C5a receptor
    • α16 contribute to the specificity of activation by the C5a receptor. Mol. Pharmacol. 47 (1995) 218-223
    • (1995) Mol. Pharmacol. , vol.47 , pp. 218-223
    • Lee, C.H.1    Katz, A.2    Simon, M.I.3
  • 73
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y., Fotiadis D., Filipek S., Saperstein D.A., Palczewski K., and Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278 (2003) 21655-21662
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 77
    • 0029589916 scopus 로고
    • Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation
    • Liu J., Conklin B.R., Blin N., Yun J., and Wess J. Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation. Proc. Natl. Acad. Sci. USA 92 (1995) 11642-11646
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 78
    • 4544338193 scopus 로고    scopus 로고
    • Perturbing the linker regions of the α-subunit of transducin: A new class of constitutively active GTP-binding proteins
    • Majumdar S., Ramachandran S., and Cerione R.A. Perturbing the linker regions of the α-subunit of transducin: A new class of constitutively active GTP-binding proteins. J. Biol. Chem. 279 (2004) 40137-40145
    • (2004) J. Biol. Chem. , vol.279 , pp. 40137-40145
    • Majumdar, S.1    Ramachandran, S.2    Cerione, R.A.3
  • 79
    • 0034695476 scopus 로고    scopus 로고
    • The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction
    • Marin E.P., Krishna A.G., Zvyaga T.A., Isele J., Siebert F., and Sakmar T.P. The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction. J. Biol. Chem. 275 (2000) 1930-1936
    • (2000) J. Biol. Chem. , vol.275 , pp. 1930-1936
    • Marin, E.P.1    Krishna, A.G.2    Zvyaga, T.A.3    Isele, J.4    Siebert, F.5    Sakmar, T.P.6
  • 80
    • 0035968223 scopus 로고    scopus 로고
    • The function of interdomain interactions in controlling nucleotide exchange rates in transducin
    • Marin E.P., Krishna A.G., Archambault V., Simuni E., Fu W.Y., and Sakmar T.P. The function of interdomain interactions in controlling nucleotide exchange rates in transducin. J. Biol. Chem. 276 (2001) 23873-23880
    • (2001) J. Biol. Chem. , vol.276 , pp. 23873-23880
    • Marin, E.P.1    Krishna, A.G.2    Archambault, V.3    Simuni, E.4    Fu, W.Y.5    Sakmar, T.P.6
  • 81
    • 0346755948 scopus 로고    scopus 로고
    • Rapid activation of transducin by mutations distant from the nucleotide-binding site. Evidence for a mechanistic model of receptor-catalyzed nucleotide exchange by G proteins
    • Marin E.P., Krishna A.G., and Sakmar T.P. Rapid activation of transducin by mutations distant from the nucleotide-binding site. Evidence for a mechanistic model of receptor-catalyzed nucleotide exchange by G proteins. J. Biol. Chem. 276 (2001) 27400-27405
    • (2001) J. Biol. Chem. , vol.276 , pp. 27400-27405
    • Marin, E.P.1    Krishna, A.G.2    Sakmar, T.P.3
  • 82
    • 0037018839 scopus 로고    scopus 로고
    • Disruption of the α5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange
    • Marin E.P., Krishna A.G., and Sakmar T.P. Disruption of the α5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange. Biochemistry 41 (2002) 6988-6994
    • (2002) Biochemistry , vol.41 , pp. 6988-6994
    • Marin, E.P.1    Krishna, A.G.2    Sakmar, T.P.3
  • 83
    • 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. Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library. J. Biol. Chem. 271 (1996) 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
  • 84
    • 0029969175 scopus 로고    scopus 로고
    • Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin
    • Mazzoni M.R., and Hamm H.E. Interaction of transducin with light-activated rhodopsin protects it from proteolytic digestion by trypsin. J. Biol. Chem. 271 (1996) 30034-30040
    • (1996) J. Biol. Chem. , vol.271 , pp. 30034-30040
    • Mazzoni, M.R.1    Hamm, H.E.2
  • 86
    • 21644449969 scopus 로고    scopus 로고
    • Functional selectivity of G protein signaling by agonist peptides and thrombin for the protease-activated receptor-1
    • McLaughlin J.N., Shen L., Holinstat M., Brooks J.D., Dibenedetto E., and Hamm H.E. Functional selectivity of G protein signaling by agonist peptides and thrombin for the protease-activated receptor-1. J. Biol. Chem. 280 (2005) 25048-25059
    • (2005) J. Biol. Chem. , vol.280 , pp. 25048-25059
    • McLaughlin, J.N.1    Shen, L.2    Holinstat, M.3    Brooks, J.D.4    Dibenedetto, E.5    Hamm, H.E.6
  • 87
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • Milligan G. G protein-coupled receptor dimerization: Function and ligand pharmacology. Mol. Pharmacol. 66 (2004) 1-7
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1-7
    • Milligan, G.1
  • 90
    • 33644835080 scopus 로고    scopus 로고
    • Regions in the G protein γ subunit important for interaction with receptors and effectors
    • Myung C.S., Lim W.K., Defilippo J., Yasuda H., Neubig R., and Garrison J.C. Regions in the G protein γ subunit important for interaction with receptors and effectors. Mol. Pharmacol. 69 (2005) 877-887
    • (2005) Mol. Pharmacol. , vol.69 , pp. 877-887
    • Myung, C.S.1    Lim, W.K.2    Defilippo, J.3    Yasuda, H.4    Neubig, R.5    Garrison, J.C.6
  • 91
    • 30044447642 scopus 로고    scopus 로고
    • The carboxyl terminus of the Gα-subunit is the latch for triggered activation of heterotrimeric G proteins
    • Nanoff C., Koppensteiner R., Yang Q., Fuerst E., Ahorn H., and Freissmuth M. The carboxyl terminus of the Gα-subunit is the latch for triggered activation of heterotrimeric G proteins. Mol. Pharmacol. 69 (2006) 397-405
    • (2006) Mol. Pharmacol. , vol.69 , pp. 397-405
    • Nanoff, C.1    Koppensteiner, R.2    Yang, Q.3    Fuerst, E.4    Ahorn, H.5    Freissmuth, M.6
  • 93
    • 0035085209 scopus 로고    scopus 로고
    • Probing the mechanism of rhodopsin-catalyzed transducin activation
    • Natochin M., Moussaif M., and Artemyev N.O. Probing the mechanism of rhodopsin-catalyzed transducin activation. J. Neurochem. 77 (2001) 202-210
    • (2001) J. Neurochem. , vol.77 , pp. 202-210
    • Natochin, M.1    Moussaif, M.2    Artemyev, N.O.3
  • 94
    • 0141733156 scopus 로고    scopus 로고
    • Rhodopsin determinants for transducin activation: A gain-of-function approach
    • Natochin M., Gasimov K.G., Moussaif M., and Artemyev N.O. Rhodopsin determinants for transducin activation: A gain-of-function approach. J. Biol. Chem. 278 (2003) 37574-37581
    • (2003) J. Biol. Chem. , vol.278 , pp. 37574-37581
    • Natochin, M.1    Gasimov, K.G.2    Moussaif, M.3    Artemyev, N.O.4
  • 95
    • 0042165824 scopus 로고    scopus 로고
    • Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor
    • Nikiforovich G.V., and Marshall G.R. Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor. Biochemistry 42 (2003) 9110-9120
    • (2003) Biochemistry , vol.42 , pp. 9110-9120
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 96
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel J.P., Hamm H.E., and Sigler P.B. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366 (1993) 654-663
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 98
    • 0033452126 scopus 로고    scopus 로고
    • A low resolution model for the interaction of G proteins with G protein-coupled receptors
    • Oliveira L., Paiva A.C., and Vriend G. A low resolution model for the interaction of G proteins with G protein-coupled receptors. Protein Eng. 12 (1999) 1087-1095
    • (1999) Protein Eng. , vol.12 , pp. 1087-1095
    • Oliveira, L.1    Paiva, A.C.2    Vriend, G.3
  • 99
  • 100
    • 0029569117 scopus 로고
    • tα on rhodopsin and guanine nucleotide binding
    • tα on rhodopsin and guanine nucleotide binding. J. Biol. Chem. 270 (1995) 31052-31058
    • (1995) J. Biol. Chem. , vol.270 , pp. 31052-31058
    • Osawa, S.1    Weiss, E.R.2
  • 101
    • 27444441027 scopus 로고    scopus 로고
    • A switch 3 point mutation in the α subunit of transducin yields a unique dominant-negative inhibitor
    • Pereira R., and Cerione R.A. A switch 3 point mutation in the α subunit of transducin yields a unique dominant-negative inhibitor. J. Biol. Chem. 280 (2005) 35696-35703
    • (2005) J. Biol. Chem. , vol.280 , pp. 35696-35703
    • Pereira, R.1    Cerione, R.A.2
  • 102
    • 22944487986 scopus 로고    scopus 로고
    • Multiple signaling states of G-protein-coupled receptors
    • Perez D.M., and Karnik S.S. Multiple signaling states of G-protein-coupled receptors. Pharmacol. Rev. 57 (2005) 147-161
    • (2005) Pharmacol. Rev. , vol.57 , pp. 147-161
    • Perez, D.M.1    Karnik, S.S.2
  • 103
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor
    • Perez D.M., Hwa J., Gaivin R., Mathur M., Brown F., and Graham R.M. Constitutive activation of a single effector pathway: Evidence for multiple activation states of a G protein-coupled receptor. Mol. Pharmacol. 49 (1996) 112-122
    • (1996) Mol. Pharmacol. , vol.49 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 105
    • 0033531794 scopus 로고    scopus 로고
    • i heterotrimers of different βγ subunit composition in Sf9 insect cell membranes
    • i heterotrimers of different βγ subunit composition in Sf9 insect cell membranes. J. Biol. Chem. 274 (1999) 13525-13533
    • (1999) J. Biol. Chem. , vol.274 , pp. 13525-13533
    • Richardson, M.1    Robishaw, J.D.2
  • 107
    • 0026655036 scopus 로고
    • Specificity of G protein β and γ subunit interactions
    • Schmidt C.J., Thomas T.C., Levine M.A., and Neer E.J. Specificity of G protein β and γ subunit interactions. J. Biol. Chem. 267 (1992) 13807-13810
    • (1992) J. Biol. Chem. , vol.267 , pp. 13807-13810
    • Schmidt, C.J.1    Thomas, T.C.2    Levine, M.A.3    Neer, E.J.4
  • 108
    • 0028172104 scopus 로고
    • sα mutant in a patient with albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase
    • sα mutant in a patient with albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J. Biol. Chem. 269 (1994) 25387-25391
    • (1994) J. Biol. Chem. , vol.269 , pp. 25387-25391
    • Schwindinger, W.F.1    Miric, A.2    Zimmerman, D.3    Levine, M.A.4
  • 109
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh S.P., Zvyaga T.A., Lichtarge O., Sakmar T.P., and Bourne H.R. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383 (1996) 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
  • 110
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon M.I., Strathmann M.P., and Gautam N. Diversity of G proteins in signal transduction. Science 252 (1991) 802-808
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 111
    • 0348010316 scopus 로고    scopus 로고
    • Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein α-subunits for selective coupling
    • Slessareva J.E., Ma H., Depree K.M., Flood L.A., Bae H., Cabrera-Vera T.M., Hamm H.E., and Graber S.G. Closely related G-protein-coupled receptors use multiple and distinct domains on G-protein α-subunits for selective coupling. J. Biol. Chem. 278 (2003) 50530-50536
    • (2003) J. Biol. Chem. , vol.278 , pp. 50530-50536
    • Slessareva, J.E.1    Ma, H.2    Depree, K.M.3    Flood, L.A.4    Bae, H.5    Cabrera-Vera, T.M.6    Hamm, H.E.7    Graber, S.G.8
  • 112
    • 2342462804 scopus 로고    scopus 로고
    • Interaction of class A G protein-coupled receptors with G proteins
    • Slusarz R., and Ciarkowski J. Interaction of class A G protein-coupled receptors with G proteins. Acta Biochim. Pol. 51 (2004) 129-136
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 129-136
    • Slusarz, R.1    Ciarkowski, J.2
  • 113
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein βγ dimer at 2.1 Å resolution
    • Sondek J., Bohm A., Lambright D.G., Hamm H.E., and Sigler P.B. Crystal structure of a G-protein βγ dimer at 2.1 Å resolution. Nature 379 (1996) 369-374
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 116
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gβ. 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. Receptor and membrane interaction sites on Gβ. A receptor-derived peptide binds to the carboxyl terminus. J. Biol. Chem. 271 (1996) 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
  • 117
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 (2001) 7761-7772
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 118
    • 0027491658 scopus 로고
    • o subunit: Mutation of conserved cysteines identifies a subunit contact surface and alters GDP affinity
    • o subunit: Mutation of conserved cysteines identifies a subunit contact surface and alters GDP affinity. Proc. Natl. Acad. Sci. USA 90 (1993) 10295-10298
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10295-10298
    • Thomas, T.C.1    Schmidt, C.J.2    Neer, E.J.3
  • 119
    • 0034741603 scopus 로고    scopus 로고
    • An intramolecular contact in Ga transducin that participates in maintaining its intrinsic GDP release rate
    • Thomas T.O., Bae H., Medkova M., and Hamm H.E. An intramolecular contact in Ga transducin that participates in maintaining its intrinsic GDP release rate. Mol. Cell Biol. Res. Commun. 4 (2001) 282-291
    • (2001) Mol. Cell Biol. Res. Commun. , vol.4 , pp. 282-291
    • Thomas, T.O.1    Bae, H.2    Medkova, M.3    Hamm, H.E.4
  • 121
    • 0033551149 scopus 로고    scopus 로고
    • A mutation in the heterotrimeric stimulatory guanine nucleotide binding protein α-subunit with impaired receptor-mediated activation because of elevated GTPase activity
    • Warner D.R., and Weinstein L.S. A mutation in the heterotrimeric stimulatory guanine nucleotide binding protein α-subunit with impaired receptor-mediated activation because of elevated GTPase activity. Proc. Natl. Acad. Sci. USA 96 (1999) 4268-4272
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4268-4272
    • Warner, D.R.1    Weinstein, L.S.2
  • 122
    • 0032508659 scopus 로고    scopus 로고
    • sα in a patient with albright hereditary osteodystrophy impairs GDP binding and receptor activation
    • sα in a patient with albright hereditary osteodystrophy impairs GDP binding and receptor activation. J. Biol. Chem. 273 (1998) 23976-23983
    • (1998) J. Biol. Chem. , vol.273 , pp. 23976-23983
    • Warner, D.R.1    Weng, G.2    Yu, S.3    Matalon, R.4    Weinstein, L.S.5
  • 123
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • Wess J. G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11 (1997) 346-354
    • (1997) FASEB J. , vol.11 , pp. 346-354
    • Wess, J.1
  • 124
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • Wess J. Molecular basis of receptor/G-protein-coupling selectivity. Pharmacol. Ther. 80 (1998) 231-264
    • (1998) Pharmacol. Ther. , vol.80 , pp. 231-264
    • Wess, J.1
  • 125
    • 0022347238 scopus 로고
    • Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site
    • West Jr. R.E., Moss J., Vaughan M., Liu T., and Liu T.Y. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. J. Biol. Chem. 260 (1985) 14428-14430
    • (1985) J. Biol. Chem. , vol.260 , pp. 14428-14430
    • West Jr., R.E.1    Moss, J.2    Vaughan, M.3    Liu, T.4    Liu, T.Y.5


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