메뉴 건너뛰기




Volumn 550, Issue 7677, 2017, Pages 543-547

Single-molecule imaging reveals receptor-G protein interactions at cell surface hot spots

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; NANOBODY; ADRENERGIC RECEPTOR; CLATHRIN; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 85032447340     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature24264     Document Type: Article
Times cited : (260)

References (24)
  • 2
    • 28644443374 scopus 로고    scopus 로고
    • Dynamics of receptor/G protein coupling in living cells
    • Hein, P., Frank, M., Hoffmann, C., Lohse, M. J. & Bönemann, M. Dynamics of receptor/G protein coupling in living cells. EMBO J. 24, 4106-4114 (2005).
    • (2005) EMBO J , vol.24 , pp. 4106-4114
    • Hein, P.1    Frank, M.2    Hoffmann, C.3    Lohse, M.J.4    Bönemann, M.5
  • 3
    • 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
  • 4
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-proteincoupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro, D. et al. Single-molecule analysis of fluorescently labeled G-proteincoupled receptors reveals complexes with distinct dynamics and organization. Proc. Natl Acad. Sci. USA 110, 743-748 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 743-748
    • Calebiro, D.1
  • 5
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler, A. et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21, 86-89 (2003).
    • (2003) Nat. Biotechnol , vol.21 , pp. 86-89
    • Keppler, A.1
  • 6
    • 39149145486 scopus 로고    scopus 로고
    • An engineered protein tag for multiprotein labeling in living cells
    • Gautier, A. et al. An engineered protein tag for multiprotein labeling in living cells. Chem. Biol. 15, 128-136 (2008).
    • (2008) Chem. Biol , vol.15 , pp. 128-136
    • Gautier, A.1
  • 7
    • 70350763863 scopus 로고    scopus 로고
    • Fractional Brownian motion versus the continuous-Time random walk: A simple test for subdiffusive dynamics
    • Magdziarz, M., Weron, A., Burnecki, K. & Klafter, J. Fractional Brownian motion versus the continuous-Time random walk: A simple test for subdiffusive dynamics. Phys. Rev. Lett. 103, 180602 (2009).
    • (2009) Phys. Rev. Lett , vol.103 , pp. 180602
    • Magdziarz, M.1    Weron, A.2    Burnecki, K.3    Klafter, J.4
  • 8
    • 84874642927 scopus 로고    scopus 로고
    • Extracting intracellular diffusive states and transition rates from single-molecule tracking data
    • Persson, F., Lindén, M., Unoson, C. & Elf, J. Extracting intracellular diffusive states and transition rates from single-molecule tracking data. Nat. Methods 10, 265-269 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 265-269
    • Persson, F.1    Lindén, M.2    Unoson, C.3    Elf, J.4
  • 9
    • 84934276305 scopus 로고    scopus 로고
    • InferenceMAP: Mapping of single-molecule dynamics with Bayesian inference
    • El Beheiry, M., Dahan, M. & Masson, J.-B. InferenceMAP: mapping of single-molecule dynamics with Bayesian inference. Nat. Methods 12, 594-595 (2015).
    • (2015) Nat. Methods , vol.12 , pp. 594-595
    • El Beheiry, M.1    Dahan, M.2    Masson, J.-B.3
  • 10
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs. Fluorescence correlation spectroscopy
    • Kusumi, A., Shirai, Y. M., Koyama-Honda, I., Suzuki, K. G. & Fujiwara, T. K. Hierarchical organization of the plasma membrane: investigations by single-molecule tracking vs. fluorescence correlation spectroscopy. FEBS Lett. 584, 1814-1823 (2010).
    • (2010) FEBS Lett , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 11
    • 0036479228 scopus 로고    scopus 로고
    • Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells
    • Scott, M. G., Benmerah, A., Muntaner, O. & Marullo, S. Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells. J. Biol. Chem. 277, 3552-3559 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 3552-3559
    • Scott, M.G.1    Benmerah, A.2    Muntaner, O.3    Marullo, S.4
  • 12
    • 33747179417 scopus 로고    scopus 로고
    • Imaging intracellular fluorescent proteins at nanometer resolution
    • Betzig, E. et al. Imaging intracellular fluorescent proteins at nanometer resolution. Science 313, 1642-1645 (2006).
    • (2006) Science , vol.313 , pp. 1642-1645
    • Betzig, E.1
  • 14
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen, S. G. et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 477, 549-555 (2011).
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.1
  • 15
    • 84875604499 scopus 로고    scopus 로고
    • Conformational biosensors reveal GPCR signalling from endosomes
    • Irannejad, R. et al. Conformational biosensors reveal GPCR signalling from endosomes. Nature 495, 534-538 (2013).
    • (2013) Nature , vol.495 , pp. 534-538
    • Irannejad, R.1
  • 16
    • 27844442717 scopus 로고    scopus 로고
    • Compartmentation of G-protein-coupled receptors and their signalling components in lipid rafts and caveolae
    • Insel, P. A. et al. Compartmentation of G-protein-coupled receptors and their signalling components in lipid rafts and caveolae. Biochem. Soc. Trans. 33, 1131-1134 (2005).
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1131-1134
    • Insel, P.A.1
  • 17
    • 54049106162 scopus 로고    scopus 로고
    • Cholesterol-dependent separation of the β2-Adrenergic receptor from its partners determines signaling efficacy: Insight into nanoscale organization of signal transduction
    • Pontier, S. M. et al. Cholesterol-dependent separation of the β2-Adrenergic receptor from its partners determines signaling efficacy: insight into nanoscale organization of signal transduction. J. Biol. Chem. 283, 24659-24672 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 24659-24672
    • Pontier, S.M.1
  • 18
    • 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
  • 19
    • 33746871075 scopus 로고    scopus 로고
    • Heterotrimeric G proteins form stable complexes with adenylyl cyclase and Kir3.1 channels in living cells
    • Rebois, R. V. et al. Heterotrimeric G proteins form stable complexes with adenylyl cyclase and Kir3.1 channels in living cells. J. Cell Sci. 119, 2807-2818
    • J. Cell Sci , vol.119 , pp. 2807-2818
    • Rebois, R.V.1
  • 20
    • 80053141840 scopus 로고    scopus 로고
    • Structural flexibility of the Gαs α-helical domain in the β2-Adrenoceptor Gs complex
    • Westfield, G. H. et al. Structural flexibility of the Gαs α-helical domain in the β2-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
  • 21
    • 84932647495 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange in heterotrimeric G proteins
    • Dror, R. O. et al. 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
  • 22
    • 85022054938 scopus 로고    scopus 로고
    • Single-molecule analysis of ligand efficacy in β2AR-Gprotein activation
    • Gregorio, G. G. et al. Single-molecule analysis of ligand efficacy in β2AR-Gprotein activation. Nature 547, 68-73 (2017).
    • (2017) Nature , vol.547 , pp. 68-73
    • Gregorio, G.G.1
  • 23
    • 84906088654 scopus 로고    scopus 로고
    • Position of transmembrane helix 6 determines receptor G protein coupling specificity
    • Rose, A. S. et al. Position of transmembrane helix 6 determines receptor G protein coupling specificity. J. Am. Chem. Soc. 136, 11244-11247 (2014).
    • (2014) J. Am. Chem. Soc , vol.136 , pp. 11244-11247
    • Rose, A.S.1
  • 24
    • 33747739472 scopus 로고    scopus 로고
    • Molecular basis of partial agonism at the neurotransmitter α2A-Adrenergic receptor and Gi-protein heterotrimer
    • Nikolaev, V. O., Hoffmann, C., Bonemann, M., Lohse, M. J. & Vilardaga, J. P. Molecular basis of partial agonism at the neurotransmitter α2A-Adrenergic receptor and Gi-protein heterotrimer. J. Biol. Chem. 281, 24506-24511 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 24506-24511
    • Nikolaev, V.O.1    Hoffmann, C.2    Bönemann, M.3    Lohse, M.J.4    Vilardaga, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.