메뉴 건너뛰기




Volumn 547, Issue 7661, 2017, Pages 68-73

Single-molecule analysis of ligand efficacy in β2AR-G-protein activation

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; FLUORESCENT DYE; G PROTEIN COUPLED RECEPTOR; NUCLEOTIDE; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; CLENBUTEROL; EPINEPHRINE; GUANOSINE DIPHOSPHATE; LIGAND; STIMULATORY GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 85022054938     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature22354     Document Type: Article
Times cited : (253)

References (35)
  • 2
    • 66649110614 scopus 로고    scopus 로고
    • GPCR and G proteins: Drug efficacy and activation in live cells
    • Vilardaga, J. P. et al. GPCR and G proteins: drug efficacy and activation in live cells. Mol. Endocrinol. 23, 590-599 (2009).
    • (2009) Mol. Endocrinol. , vol.23 , pp. 590-599
    • Vilardaga, J.P.1
  • 3
    • 84872369895 scopus 로고    scopus 로고
    • New concepts in pharmacological efficacy at 7TM receptors: IUPHAR review 2
    • Kenakin, T. New concepts in pharmacological efficacy at 7TM receptors: IUPHAR review 2. Br. J. Pharmacol. 168, 554-575 (2013).
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 554-575
    • Kenakin, T.1
  • 4
    • 84893980520 scopus 로고    scopus 로고
    • The role of protein dynamics in GPCR function: Insights from the β 2AR and rhodopsin
    • Manglik, A. & Kobilka, B. The role of protein dynamics in GPCR function: insights from the β 2AR and rhodopsin. Curr. Opin. Cell Biol. 27, 136-143 (2014).
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 136-143
    • Manglik, A.1    Kobilka, B.2
  • 5
    • 77953185520 scopus 로고    scopus 로고
    • The selectivity of β-adrenoceptor agonists at human β 1-, β 2-and β 3-adrenoceptors
    • Baker, J. G. The selectivity of β-adrenoceptor agonists at human β 1-, β 2-and β 3-adrenoceptors. Br. J. Pharmacol. 160, 1048-1061 (2010).
    • (2010) Br. J. Pharmacol. , vol.160 , pp. 1048-1061
    • Baker, J.G.1
  • 6
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β 2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. et al. Crystal structure of the β 2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 7
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • Kruse, A. C. et al. Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504, 101-106 (2013).
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1
  • 8
    • 84939795137 scopus 로고    scopus 로고
    • Structural insights into μ-opioid receptor activation
    • Huang, W. et al. Structural insights into μ-opioid receptor activation. Nature 524, 315-321 (2015).
    • (2015) Nature , vol.524 , pp. 315-321
    • Huang, W.1
  • 9
    • 84982803363 scopus 로고    scopus 로고
    • Structure of the adenosine A2A receptor bound to an engineered G protein
    • Carpenter, B., Nehmé, R., Warne, T., Leslie, A. G. & Tate, C. G. Structure of the adenosine A2A receptor bound to an engineered G protein. Nature 536, 104-107 (2016).
    • (2016) Nature , vol.536 , pp. 104-107
    • Carpenter, B.1    Nehmé, R.2    Warne, T.3    Leslie, A.G.4    Tate, C.G.5
  • 10
    • 67249125561 scopus 로고    scopus 로고
    • The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex
    • Yao, X. J. et al. The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. Proc. Natl Acad. Sci. USA 106, 9501-9506 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 9501-9506
    • Yao, X.J.1
  • 11
    • 84930226866 scopus 로고    scopus 로고
    • Structural insights into the dynamic process of β 2-adrenergic receptor signaling
    • Manglik, A. et al. Structural insights into the dynamic process of β 2-adrenergic receptor signaling. Cell 161, 1101-1111 (2015).
    • (2015) Cell , vol.161 , pp. 1101-1111
    • Manglik, A.1
  • 12
    • 84873298278 scopus 로고    scopus 로고
    • The dynamic process of β 2-adrenergic receptor activation
    • Nygaard, R. et al. The dynamic process of β 2-adrenergic receptor activation. Cell 152, 532-542 (2013).
    • (2013) Cell , vol.152 , pp. 532-542
    • Nygaard, R.1
  • 13
    • 3543051291 scopus 로고    scopus 로고
    • Cy3B: Improving the performance of cyanine dyes
    • Cooper, M. et al. Cy3B: improving the performance of cyanine dyes. J. Fluoresc. 14, 145-150 (2004).
    • (2004) J. Fluoresc. , vol.14 , pp. 145-150
    • Cooper, M.1
  • 14
    • 84940478169 scopus 로고    scopus 로고
    • Conformational dynamics of a class C G-protein-coupled receptor
    • Vafabakhsh, R., Levitz, J. & Isacoff, E. Y. Conformational dynamics of a class C G-protein-coupled receptor. Nature 524, 497-501 (2015).
    • (2015) Nature , vol.524 , pp. 497-501
    • Vafabakhsh, R.1    Levitz, J.2    Isacoff, E.Y.3
  • 15
    • 0037006790 scopus 로고    scopus 로고
    • Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
    • Kim, H. D. et al. Mg2+-dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules. Proc. Natl Acad. Sci. USA 99, 4284-4289 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 4284-4289
    • Kim, H.D.1
  • 16
    • 84961177760 scopus 로고    scopus 로고
    • Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β 2AR
    • Lamichhane, R. et al. Single-molecule view of basal activity and activation mechanisms of the G protein-coupled receptor β 2AR. Proc. Natl Acad. Sci. USA 112, 14254-14259 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 14254-14259
    • Lamichhane, R.1
  • 17
    • 0028987954 scopus 로고
    • Physiological effects of inverse agonists in transgenic mice with myocardial overexpression of the β 2-adrenoceptor
    • Bond, R. A. et al. Physiological effects of inverse agonists in transgenic mice with myocardial overexpression of the β 2-adrenoceptor. Nature 374, 272-276 (1995).
    • (1995) Nature , vol.374 , pp. 272-276
    • Bond, R.A.1
  • 18
    • 84947747592 scopus 로고    scopus 로고
    • Functional dynamics within the human ribosome regulate the rate of active protein synthesis
    • Ferguson, A. et al. Functional dynamics within the human ribosome regulate the rate of active protein synthesis. Mol. Cell 60, 475-486 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 475-486
    • Ferguson, A.1
  • 19
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • Galés, C. et al. Real-time monitoring of receptor and G-protein interactions in living cells. Nat. Methods 2, 177-184 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 177-184
    • Galés, C.1
  • 20
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst, O. P., Gramse, V., Kolbe, M., Hofmann, K. P. & Heck, M. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl Acad. Sci. USA 104, 10859-10864 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 21
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T. W. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140, 1-22 (1994).
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 22
    • 33845942468 scopus 로고    scopus 로고
    • Gs activation is time-limiting in initiating receptor-mediated signaling
    • Hein, P. et al. Gs activation is time-limiting in initiating receptor-mediated signaling. J. Biol. Chem. 281, 33345-33351 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 33345-33351
    • Hein, P.1
  • 23
    • 33748355624 scopus 로고    scopus 로고
    • Probing the activation-promoted structural rearrangements in preassembled receptor-G-protein complexes
    • Galés, C. et al. Probing the activation-promoted structural rearrangements in preassembled receptor-G-protein complexes. Nat. Struct. Mol. Biol. 13, 778-786 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 778-786
    • Galés, C.1
  • 24
    • 80052969688 scopus 로고    scopus 로고
    • Inactive-state preassembly of Gq-coupled receptors and Gq heterotrimers
    • Qin, K., Dong, C., Wu, G. & Lambert, N. A. Inactive-state preassembly of Gq-coupled receptors and Gq heterotrimers. Nat. Chem. Biol. 7, 740-747 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 740-747
    • Qin, K.1    Dong, C.2    Wu, G.3    Lambert, N.A.4
  • 25
    • 80053141840 scopus 로고    scopus 로고
    • Structural flexibility of the Gα s α-helical domain in the β 2-adrenoceptor Gs complex
    • Westfield, G. H. et al. Structural flexibility of the Gα s α-helical domain in the β 2-adrenoceptor Gs complex. Proc. Natl Acad. Sci. USA 108, 16086-16091 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 16086-16091
    • Westfield, G.H.1
  • 26
    • 84922309763 scopus 로고    scopus 로고
    • Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex
    • Damian, M. et al. Ghrelin receptor conformational dynamics regulate the transition from a preassembled to an active receptor:Gq complex. Proc. Natl Acad. Sci. USA 112, 1601-1606 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 1601-1606
    • Damian, M.1
  • 27
    • 0021289119 scopus 로고
    • [3H]GDP release from rat and hamster adipocyte membranes independently linked to receptors involved in activation or inhibition of adenylate cyclase. Differential susceptibility to two bacterial toxins
    • Murayama, T. & Ui, M. [3H]GDP release from rat and hamster adipocyte membranes independently linked to receptors involved in activation or inhibition of adenylate cyclase. Differential susceptibility to two bacterial toxins. J. Biol. Chem. 259, 761-769 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 761-769
    • Murayama, T.1    Ui, M.2
  • 28
    • 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. & Weinstein, H. Molecular dynamics simulations of transducin: interdomain and front to back communication in activation and nucleotide exchange. J. Mol. Biol. 338, 469-481 (2004).
    • (2004) J. Mol. Biol. , vol.338 , pp. 469-481
    • Ceruso, M.A.1    Periole, X.2    Weinstein, H.3
  • 29
    • 2642588172 scopus 로고    scopus 로고
    • Sequence of interactions in receptor-G-protein coupling
    • Herrmann, R. et al. Sequence of interactions in receptor-G-protein coupling. J. Biol. Chem. 279, 24283-24290 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 24283-24290
    • Herrmann, R.1
  • 30
    • 33750615086 scopus 로고    scopus 로고
    • Rhodopsin-transducin coupling: Role of the Gα C-terminus in nucleotide exchange catalysis
    • Herrmann, R. et al. Rhodopsin-transducin coupling: role of the Gα C-terminus in nucleotide exchange catalysis. Vision Res. 46, 4582-4593 (2006).
    • (2006) Vision Res. , vol.46 , pp. 4582-4593
    • Herrmann, R.1
  • 32
    • 70349810683 scopus 로고    scopus 로고
    • Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins
    • Kapoor, N., Menon, S. T., Chauhan, R., Sachdev, P. & Sakmar, T. P. Structural evidence for a sequential release mechanism for activation of heterotrimeric G proteins. J. Mol. Biol. 393, 882-897 (2009).
    • (2009) J. Mol. Biol. , vol.393 , pp. 882-897
    • Kapoor, N.1    Menon, S.T.2    Chauhan, R.3    Sachdev, P.4    Sakmar, T.P.5
  • 33
    • 84906860677 scopus 로고    scopus 로고
    • A conserved phenylalanine as a relay between the α 5 helix and the GDP binding region of heterotrimeric Gi protein α subunit
    • Kaya, A. I. et al. A conserved phenylalanine as a relay between the α 5 helix and the GDP binding region of heterotrimeric Gi protein α subunit. J. Biol. Chem. 289, 24475-24487 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 24475-24487
    • Kaya, A.I.1
  • 34
    • 84932647495 scopus 로고    scopus 로고
    • Signal transduction. Structural basis for nucleotide exchange in heterotrimeric G proteins
    • Dror, R. O. et al. Signal transduction. Structural basis for nucleotide exchange in heterotrimeric G proteins. Science 348, 1361-1365 (2015).
    • (2015) Science , vol.348 , pp. 1361-1365
    • Dror, R.O.1
  • 35
    • 84939522532 scopus 로고    scopus 로고
    • Universal allosteric mechanism for Gα activation by GPCRs
    • Flock, T. et al. Universal allosteric mechanism for Gα activation by GPCRs. Nature 524, 173-179 (2015).
    • (2015) Nature , vol.524 , pp. 173-179
    • Flock, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.