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Volumn 289, Issue 41, 2014, Pages 28271-28283

Allosteric modulation of β-arrestin-biased angiotensin II type 1 receptor signaling by membrane stretch

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHEMICAL ACTIVATION; LIGANDS; OSMOSIS; SCAFFOLDS (BIOLOGY);

EID: 84907821993     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.585067     Document Type: Article
Times cited : (57)

References (55)
  • 2
    • 84888122574 scopus 로고    scopus 로고
    • Solving the cardiac hypertrophy riddle: The angiotensin ii-mechanical stress connection
    • Zablocki, D., and Sadoshima, J. (2013) Solving the cardiac hypertrophy riddle: The angiotensin II-mechanical stress connection. Circ. Res. 113, 1192-1195
    • (2013) Circ. Res , vol.113 , pp. 1192-1195
    • Zablocki, D.1    Sadoshima, J.2
  • 3
    • 58049196875 scopus 로고    scopus 로고
    • Neurosensory mechanotransduction
    • Chalfie, M. (2009) Neurosensory mechanotransduction. Nat. Rev. Mol. Cell Biol. 10, 44-52
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 44-52
    • Chalfie, M.1
  • 4
    • 0036889937 scopus 로고    scopus 로고
    • Myogenic tone, reactivity, and forced dilatation: A three-phase model of in vitro arterial myogenic behavior
    • Osol, G., Brekke, J. F., McElroy-Yaggy, K., and Gokina, N. I. (2002) Myogenic tone, reactivity, and forced dilatation: a three-phase model of in vitro arterial myogenic behavior. Am. J. Physiol. Heart Circ. Physiol. 283, H2260-H2267
    • (2002) Am. J. Physiol. Heart Circ. Physiol , vol.283 , pp. H2260-H2267
    • Osol, G.1    Brekke, J.F.2    McElroy-Yaggy, K.3    Gokina, N.I.4
  • 6
    • 77953819826 scopus 로고    scopus 로고
    • β-Arrestin-biased agonism of the angiotensin receptor induced by mechanical stress
    • Rakesh, K., Yoo, B., Kim, I. M., Salazar, N., Kim, K. S., and Rockman, H. A. (2010) β-Arrestin-biased agonism of the angiotensin receptor induced by mechanical stress. Sci. Signal. 3, ra46
    • (2010) Sci. Signal , vol.3 , pp. ra46
    • Rakesh, K.1    Yoo, B.2    Kim, I.M.3    Salazar, N.4    Kim, K.S.5    Rockman, H.A.6
  • 9
    • 77951844975 scopus 로고    scopus 로고
    • Teaching old receptors new tricks: Biasing seven-transmembrane receptors
    • Rajagopal, S., Rajagopal, K., and Lefkowitz, R. J. (2010) Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 9, 373-386
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 373-386
    • Rajagopal, S.1    Rajagopal, K.2    Lefkowitz, R.J.3
  • 10
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors
    • Reiter, E., Ahn, S., Shukla, A. K., and Lefkowitz, R. J. (2012) Molecular mechanism of β-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52, 179-197
    • (2012) Annu. Rev. Pharmacol. Toxicol , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 14
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 a crystal structure
    • 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
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 16
    • 33750366860 scopus 로고    scopus 로고
    • G protein-coupled receptors sense fluid shear stress in endothelial cells
    • Chachisvilis, M., Zhang, Y. L., and Frangos, J. A. (2006) G protein-coupled receptors sense fluid shear stress in endothelial cells. Proc. Natl. Acad. Sci. U.S.A. 103, 15463-15468
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15463-15468
    • Chachisvilis, M.1    Zhang, Y.L.2    Frangos, J.A.3
  • 21
    • 0027513982 scopus 로고
    • A mutation- induced activated state of the β2-adrenergic receptor. Extending the ternary complex model
    • Samama, P., Cotecchia, S., Costa, T., and Lefkowitz, R. J. (1993) A mutation- induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 268, 4625-4636
    • (1993) J. Biol. Chem , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 22
    • 0019137579 scopus 로고
    • A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor
    • De Lean, A., Stadel, J. M., and Lefkowitz, R. J. (1980) A ternary complex model explains the agonist-specific binding properties of the adenylate cyclase-coupled β-adrenergic receptor. J. Biol. Chem. 255, 7108-7117
    • (1980) J. Biol. Chem , vol.255 , pp. 7108-7117
    • De Lean, A.1    Stadel, J.M.2    Lefkowitz, R.J.3
  • 23
    • 0030664060 scopus 로고    scopus 로고
    • Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity
    • Gurevich, V. V., Pals-Rylaarsdam, R., Benovic, J. L., Hosey, M. M., and Onorato, J. J. (1997) Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J. Biol. Chem. 272, 28849-28852
    • (1997) J. Biol. Chem , vol.272 , pp. 28849-28852
    • Gurevich, V.V.1    Pals-Rylaarsdam, R.2    Benovic, J.L.3    Hosey, M.M.4    Onorato, J.J.5
  • 24
    • 0033181342 scopus 로고    scopus 로고
    • GPCR-gα fusion proteins: Molecular analysis of receptor-g-protein coupling
    • Seifert, R., Wenzel-Seifert, K., and Kobilka, B. K. (1999) GPCR-Gα fusion proteins: molecular analysis of receptor-G-protein coupling. Trends Pharmacol. Sci. 20, 383-389
    • (1999) Trends Pharmacol. Sci , vol.20 , pp. 383-389
    • Seifert, R.1    Wenzel-Seifert, K.2    Kobilka, B.K.3
  • 26
    • 0025194765 scopus 로고
    • Characterization of adenosine a1 receptors in intact ddt1 mf-2 smooth muscle cells
    • Gerwins, P., Nordstedt, C., and Fredholm, B. B. (1990) Characterization of adenosine A1 receptors in intact DDT1 MF-2 smooth muscle cells. Mol. Pharmacol. 38, 660-666
    • (1990) Mol. Pharmacol , vol.38 , pp. 660-666
    • Gerwins, P.1    Nordstedt, C.2    Fredholm, B.B.3
  • 29
    • 17644391412 scopus 로고    scopus 로고
    • Monitoring agonistpromoted conformational changes of β-arrestin in living cells by intramolecular bret
    • Charest, P. G., Terrillon, S., and Bouvier, M. (2005) Monitoring agonistpromoted conformational changes of β-arrestin in living cells by intramolecular BRET. EMBO Rep. 6, 334-340
    • (2005) EMBO Rep , vol.6 , pp. 334-340
    • Charest, P.G.1    Terrillon, S.2    Bouvier, M.3
  • 31
    • 34548438468 scopus 로고    scopus 로고
    • Activation of g protein-coupled receptors
    • Deupi, X., and Kobilka, B. (2007) Activation of G protein-coupled receptors. Adv. Protein Chem. 74, 137-166
    • (2007) Adv. Protein Chem , vol.74 , pp. 137-166
    • Deupi, X.1    Kobilka, B.2
  • 32
    • 84864243901 scopus 로고    scopus 로고
    • Where have all the active receptor states gone?
    • Onaran, H. O., and Costa, T. (2012) Where have all the active receptor states gone? Nat. Chem. Biol. 8, 674-677
    • (2012) Nat. Chem. Biol , vol.8 , pp. 674-677
    • Onaran, H.O.1    Costa, T.2
  • 33
    • 79954425389 scopus 로고    scopus 로고
    • Structural insights into adrenergic receptor function and pharmacology
    • Kobilka, B. K. (2011) Structural insights into adrenergic receptor function and pharmacology. Trends Pharmacol. Sci. 32, 213-218
    • (2011) Trends Pharmacol. Sci , vol.32 , pp. 213-218
    • Kobilka, B.K.1
  • 34
    • 84864030656 scopus 로고    scopus 로고
    • Sensing pressure with ion channels
    • Nilius, B., and Honoré, E. (2012) Sensing pressure with ion channels. Trends Neurosci. 35, 477-486
    • (2012) Trends Neurosci , vol.35 , pp. 477-486
    • Nilius, B.1    Honoré, E.2
  • 35
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • Kung, C. (2005) A possible unifying principle for mechanosensation. Nature 436, 647-654
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 37
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos, A., and Kenakin, T. (2002) G protein-coupled receptor allosterism and complexing. Pharmacol. Rev. 54, 323-374
    • (2002) Pharmacol. Rev , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 38
    • 78149496159 scopus 로고    scopus 로고
    • Allosteric modulation of g protein-coupled receptors: A pharmacological perspective
    • Keov, P., Sexton, P. M., and Christopoulos, A. (2011) Allosteric modulation of G protein-coupled receptors: a pharmacological perspective. Neuropharmacology 60, 24-35
    • (2011) Neuropharmacology , vol.60 , pp. 24-35
    • Keov, P.1    Sexton, P.M.2    Christopoulos, A.3
  • 39
    • 0037414774 scopus 로고    scopus 로고
    • Identification of an allosteric binding site for zn2+ on the β2 adrenergic receptor
    • Swaminath, G., Lee, T. W., and Kobilka, B. (2003) Identification of an allosteric binding site for Zn2+ on the β2 adrenergic receptor. J. Biol. Chem. 278, 352-356
    • (2003) J. Biol. Chem , vol.278 , pp. 352-356
    • Swaminath, G.1    Lee, T.W.2    Kobilka, B.3
  • 42
    • 84860253205 scopus 로고    scopus 로고
    • Differential β-arrestin-dependent conformational signaling and cellular responses revealed by angiotensin analogs
    • Zimmerman, B., Beautrait, A., Aguila, B., Charles, R., Escher, E., Claing, A., Bouvier, M., and Laporte, S. A. (2012) Differential β-arrestin-dependent conformational signaling and cellular responses revealed by angiotensin analogs. Sci. Signal. 5, ra33
    • (2012) Sci. Signal , vol.5 , pp. ra33
    • Zimmerman, B.1    Beautrait, A.2    Aguila, B.3    Charles, R.4    Escher, E.5    Claing, A.6    Bouvier, M.7    Laporte, S.A.8
  • 44
    • 0025212680 scopus 로고
    • Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • Cotecchia, S., Exum, S., Caron, M. G., and Lefkowitz, R. J. (1990) Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. U.S.A. 87, 2896-2900
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 45
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active g protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • Gether, U., Ballesteros, J. A., Seifert, R., Sanders-Bush, E., Weinstein, H., and Kobilka, B. K. (1997) Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 272, 2587-2590
    • (1997) J. Biol. Chem , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 48
    • 0037022535 scopus 로고    scopus 로고
    • Signal-dependent translocation of transducin, rgs9-1-gβ5l complex, and arrestin to detergent-resistant membrane rafts in photoreceptors
    • Nair, K. S., Balasubramanian, N., and Slepak, V. Z. (2002) Signal-dependent translocation of transducin, RGS9-1-Gβ5L complex, and arrestin to detergent-resistant membrane rafts in photoreceptors. Curr. Biol. 12, 421-425
    • (2002) Curr. Biol , vol.12 , pp. 421-425
    • Nair, K.S.1    Balasubramanian, N.2    Slepak, V.Z.3
  • 49
    • 23044449837 scopus 로고    scopus 로고
    • Lipids, lipid rafts and caveolae: Their importance for gpcr signaling and their centrality to the endocannabinoid system
    • Barnett-Norris, J., Lynch, D., and Reggio, P. H. (2005) Lipids, lipid rafts and caveolae: their importance for GPCR signaling and their centrality to the endocannabinoid system. Life Sci. 77, 1625-1639
    • (2005) Life Sci , vol.77 , pp. 1625-1639
    • Barnett-Norris, J.1    Lynch, D.2    Reggio, P.H.3
  • 54
    • 0030074678 scopus 로고    scopus 로고
    • Integrative role of the lamina terminalis in the regulation of cardiovascular and body fluid homeostasis
    • Johnson, A. K., Cunningham, J. T., and Thunhorst, R. L. (1996) Integrative role of the lamina terminalis in the regulation of cardiovascular and body fluid homeostasis. Clin. Exp. Pharmacol. Physiol. 23, 183-191
    • (1996) Clin. Exp. Pharmacol. Physiol , vol.23 , pp. 183-191
    • Johnson, A.K.1    Cunningham, J.T.2    Thunhorst, R.L.3
  • 55
    • 27844583473 scopus 로고    scopus 로고
    • Divergent behavioral roles of angiotensin receptor intracellular signaling cascades
    • Daniels, D., Yee, D. K., Faulconbridge, L. F., and Fluharty, S. J. (2005) Divergent behavioral roles of angiotensin receptor intracellular signaling cascades. Endocrinology 146, 5552-5560
    • (2005) Endocrinology , vol.146 , pp. 5552-5560
    • Daniels, D.1    Yee, D.K.2    Faulconbridge, L.F.3    Fluharty, S.J.4


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