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Volumn 18, Issue 3, 2016, Pages 303-310

β-Arrestin drives MAP kinase signalling from clathrin-coated structures after GPCR dissociation

Author keywords

[No Author keywords available]

Indexed keywords

BETA 1 ADRENERGIC RECEPTOR; BETA ARRESTIN; BETA ARRESTIN 2; CLATHRIN; G PROTEIN COUPLED RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; ARRB2 PROTEIN, HUMAN; ARRESTIN3; GUANINE NUCLEOTIDE BINDING PROTEIN; RETINA S ANTIGEN;

EID: 84959245777     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3307     Document Type: Article
Times cited : (186)

References (38)
  • 1
    • 80052359992 scopus 로고    scopus 로고
    • Emerging paradigms of-arrestindependent seven transmembrane receptor signaling
    • Shukla, A. K., Xiao, K., Lefkowitz, R. J. Emerging paradigms of-arrestindependent seven transmembrane receptor signaling. Trends Biochem. Sci. 36, 457-469 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 457-469
    • Shukla, A.K.1    Xiao, K.2    Lefkowitz, R.J.3
  • 2
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated-adrenergic receptor by the-adrenergic receptor kinase: Potential role of an analog of the retinal protein arrestin (48-kDa protein)
    • Benovic, J. L. et al. Functional desensitization of the isolated-adrenergic receptor by the-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc. Natl Acad. Sci. USA 84, 8879-8882 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8879-8882
    • Benovic, J.L.1
  • 3
    • 0038487327 scopus 로고    scopus 로고
    • The ins and outs of G proteincoupled receptor trafficking
    • Marchese, A., Chen, C., Kim, Y. M., Benovic, J. L. The ins and outs of G proteincoupled receptor trafficking. Trends Biochem. Sci. 28, 369-376 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 369-376
    • Marchese, A.1    Chen, C.2    Kim, Y.M.3    Benovic, J.L.4
  • 4
    • 84906232914 scopus 로고    scopus 로고
    • Visualization of arrestin recruitment by a G-protein-coupled receptor
    • Shukla, A. K. et al. Visualization of arrestin recruitment by a G-protein-coupled receptor. Nature 512, 218-222 (2014).
    • (2014) Nature , vol.512 , pp. 218-222
    • Shukla, A.K.1
  • 5
    • 84938359988 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
    • Kang, Y. et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561-567 (2015).
    • (2015) Nature , vol.523 , pp. 561-567
    • Kang, Y.1
  • 6
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka, Y. et al. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem. 273, 685-688 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 685-688
    • Daaka, Y.1
  • 7
    • 0037458614 scopus 로고    scopus 로고
    • The stability of the G protein-coupled receptor-arrestin interaction determines the mechanism and functional consequence of ERK activation
    • Tohgo, A. et al. The stability of the G protein-coupled receptor-arrestin interaction determines the mechanism and functional consequence of ERK activation. J. Biol. Chem. 278, 6258-6267 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 6258-6267
    • Tohgo, A.1
  • 8
    • 4143070533 scopus 로고    scopus 로고
    • Differential kinetic and spatial patterns of-arrestin and G protein-mediated ERK activation by the angiotensin II receptor
    • Ahn, S., Shenoy, S. K., Wei, H., Lefkowitz, R. J. Differential kinetic and spatial patterns of-arrestin and G protein-mediated ERK activation by the angiotensin II receptor. J. Biol. Chem. 279, 35518-35525 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 35518-35525
    • Ahn, S.1    Shenoy, S.K.2    Wei, H.3    Lefkowitz, R.J.4
  • 9
    • 9144253232 scopus 로고    scopus 로고
    • Stable interaction between-arrestin 2 and angiotensin type 1A receptor is required for-arrestin 2-mediated activation of extracellular signal-regulated kinases 1 and 2
    • Wei, H., Ahn, S., Barnes, W. G., Lefkowitz, R. J. Stable interaction between-arrestin 2 and angiotensin type 1A receptor is required for-arrestin 2-mediated activation of extracellular signal-regulated kinases 1 and 2. J. Biol. Chem. 279, 48255-48261 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 48255-48261
    • Wei, H.1    Ahn, S.2    Barnes, W.G.3    Lefkowitz, R.J.4
  • 11
    • 0026539327 scopus 로고
    • Distinct regulation of-1-and-2-adrenergic receptors in Chinese hamster fibroblasts
    • Suzuki, T. et al. Distinct regulation of-1-and-2-adrenergic receptors in Chinese hamster fibroblasts. Mol. Pharmacol. 41, 542-548 (1992).
    • (1992) Mol. Pharmacol. , vol.41 , pp. 542-548
    • Suzuki, T.1
  • 12
    • 0034666323 scopus 로고    scopus 로고
    • Interaction with-arrestin determines the difference in internalization behavior between-1-and-2-adrenergic receptors
    • Shiina, T., Kawasaki, A., Nagao, T., Kurose, H. Interaction with-arrestin determines the difference in internalization behavior between-1-and-2-adrenergic receptors. J. Biol. Chem. 275, 29082-29090 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29082-29090
    • Shiina, T.1    Kawasaki, A.2    Nagao, T.3    Kurose, H.4
  • 13
    • 1342347559 scopus 로고    scopus 로고
    • Differences in endosomal targeting of human (-)1-and (-)2-adrenergic receptors following clathrinmediated endocytosis
    • Liang, W., Curran, P. K., Hoang, Q., Moreland, R. T., Fishman, P. H. Differences in endosomal targeting of human (-)1-and (-)2-adrenergic receptors following clathrinmediated endocytosis. J. Cell Sci. 117, 723-734 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 723-734
    • Liang, W.1    Curran, P.K.2    Hoang, Q.3    Moreland, R.T.4    Fishman, P.H.5
  • 14
    • 84922054440 scopus 로고    scopus 로고
    • Endophilin marks and controls a clathrin-independent endocytic pathway
    • Boucrot, E. et al. Endophilin marks and controls a clathrin-independent endocytic pathway. Nature 517, 460-465 (2015).
    • (2015) Nature , vol.517 , pp. 460-465
    • Boucrot, E.1
  • 15
    • 84908576799 scopus 로고    scopus 로고
    • Flat clathrin lattices: Stable features of the plasma membrane
    • Grove, J. et al. Flat clathrin lattices: stable features of the plasma membrane. Mol. Biol. Cell 25, 3581-3594 (2014).
    • (2014) Mol. Biol. Cell , vol.25 , pp. 3581-3594
    • Grove, J.1
  • 16
    • 34247187332 scopus 로고    scopus 로고
    • Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate
    • Zoncu, R. et al. Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate. Proc. Natl Acad. Sci. USA 104, 3793-3798 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 3793-3798
    • Zoncu, R.1
  • 18
    • 0037128214 scopus 로고    scopus 로고
    • G protein-coupled receptor/arrestin3 modulation of the endocytic machinery
    • Santini, F., Gaidarov, I., Keen, J. H. G protein-coupled receptor/arrestin3 modulation of the endocytic machinery. J. Cell Biol. 156, 665-676 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 665-676
    • Santini, F.1    Gaidarov, I.2    Keen, J.H.3
  • 19
    • 33749079184 scopus 로고    scopus 로고
    • Cargo regulates clathrin-coated pit dynamics
    • Puthenveedu, M. A., von Zastrow, M. Cargo regulates clathrin-coated pit dynamics. Cell 127, 113-124 (2006).
    • (2006) Cell , vol.127 , pp. 113-124
    • Puthenveedu, M.A.1    Von Zastrow, M.2
  • 20
    • 0026702733 scopus 로고
    • Characterization of the-adrenoceptor subtype(s) mediating the positive inotropic effects of epinine, dopamine, dobutamine, denopamine and xamoterol in isolated human right atrium
    • Deighton, N. M., Motomura, S., Bals, S., Zerkowski, H. R., Brodde, O. E. Characterization of the-adrenoceptor subtype(s) mediating the positive inotropic effects of epinine, dopamine, dobutamine, denopamine and xamoterol in isolated human right atrium. J. Pharmacol. Exp. Ther. 262, 532-538 (1992).
    • (1992) J. Pharmacol. Exp. Ther. , vol.262 , pp. 532-538
    • Deighton, N.M.1    Motomura, S.2    Bals, S.3    Zerkowski, H.R.4    Brodde, O.E.5
  • 21
    • 84856397579 scopus 로고    scopus 로고
    • Neurexin-neuroligin adhesions capture surface-diffusing AMPA receptors through PSD-95 scaffolds
    • Mondin, M. et al. Neurexin-neuroligin adhesions capture surface-diffusing AMPA receptors through PSD-95 scaffolds. J. Neurosci. 31, 13500-13515 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 13500-13515
    • Mondin, M.1
  • 22
    • 84887610283 scopus 로고    scopus 로고
    • Building a better dynasore: The dyngo compounds potently inhibit dynamin and endocytosis
    • McCluskey, A. et al. Building a better dynasore: the dyngo compounds potently inhibit dynamin and endocytosis. Traffic 14, 1272-1289 (2013).
    • (2013) Traffic , vol.14 , pp. 1272-1289
    • McCluskey, A.1
  • 23
    • 84922054440 scopus 로고    scopus 로고
    • Endophilin marks and controls a clathrin-independent endocytic pathway
    • Boucrot, E. et al. Endophilin marks and controls a clathrin-independent endocytic pathway. Nature 517, 460-465 (2015).
    • (2015) Nature , vol.517 , pp. 460-465
    • Boucrot, E.1
  • 24
    • 45549100234 scopus 로고    scopus 로고
    • Use of dynasore, the small molecule inhibitor of dynamin, in the regulation of endocytosis
    • Kirchhausen, T., Macia, E., Pelish, H. E. Use of dynasore, the small molecule inhibitor of dynamin, in the regulation of endocytosis. Methods Enzymol. 438, 77-93 (2008).
    • (2008) Methods Enzymol. , vol.438 , pp. 77-93
    • Kirchhausen, T.1    MacIa, E.2    Pelish, H.E.3
  • 25
    • 84905454446 scopus 로고    scopus 로고
    • Ligand-specific endocytic dwell times control functional selectivity of the cannabinoid receptor 1
    • Flores-Otero, J. et al. Ligand-specific endocytic dwell times control functional selectivity of the cannabinoid receptor 1. Nat. Commun. 5, 4589 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4589
    • Flores-Otero, J.1
  • 26
    • 84881544899 scopus 로고    scopus 로고
    • Advances in analysis of low signal-to-noise images link dynamin and AP2 to the functions of an endocytic checkpoint
    • Aguet, F., Antonescu, C. N., Mettlen, M., Schmid, S. L., Danuser, G. Advances in analysis of low signal-to-noise images link dynamin and AP2 to the functions of an endocytic checkpoint. Dev. Cell 26, 279-291 (2013).
    • (2013) Dev. Cell , vol.26 , pp. 279-291
    • Aguet, F.1    Antonescu, C.N.2    Mettlen, M.3    Schmid, S.L.4    Danuser, G.5
  • 27
    • 33749079184 scopus 로고    scopus 로고
    • Cargo regulates clathrin-coated pit dynamics
    • Puthenveedu, M. A., von Zastrow, M. Cargo regulates clathrin-coated pit dynamics. Cell 127, 113-124 (2006).
    • (2006) Cell , vol.127 , pp. 113-124
    • Puthenveedu, M.A.1    Von Zastrow, M.2
  • 28
    • 84866028189 scopus 로고    scopus 로고
    • Regulation of endocytic clathrin dynamics by cargo ubiquitination
    • Henry, A. G. et al. Regulation of endocytic clathrin dynamics by cargo ubiquitination. Dev. Cell 23, 519-532 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 519-532
    • Henry, A.G.1
  • 29
    • 84887572409 scopus 로고    scopus 로고
    • Extensive shape shifting underlies functional versatility of arrestins
    • Gurevich, V. V., Gurevich, E. V. Extensive shape shifting underlies functional versatility of arrestins. Curr. Opin. Cell Biol. 27, 1-9 (2014).
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 1-9
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 30
    • 0026050303 scopus 로고
    • Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin
    • Palczewski, K., Pulvermuller, A., Buczylko, J., Hofmann, K. P. Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin. J. Biol. Chem. 266, 18649-18654 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 18649-18654
    • Palczewski, K.1    Pulvermuller, A.2    Buczylko, J.3    Hofmann, K.P.4
  • 31
    • 0029770657 scopus 로고    scopus 로고
    • Arrestin acts as a clathrin adaptor in endocytosis of the-2-adrenergic receptor
    • Goodman, O. B. Jr et al.-Arrestin acts as a clathrin adaptor in endocytosis of the-2-adrenergic receptor. Nature 383, 447-450 (1996).
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman, O.B.1
  • 32
    • 0033575916 scopus 로고    scopus 로고
    • A kinaseregulated PDZ-domain interaction controls endocytic sorting of the-2-adrenergic receptor
    • Cao, T. T., Deacon, H. W., Reczek, D., Bretscher, A., von Zastrow, M. A kinaseregulated PDZ-domain interaction controls endocytic sorting of the-2-adrenergic receptor. Nature 401, 286-290 (1999).
    • (1999) Nature , vol.401 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    Von Zastrow, M.5
  • 33
    • 79957914861 scopus 로고    scopus 로고
    • SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
    • Temkin, P. et al. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nat. Cell Biol. 13, 715-721 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 715-721
    • Temkin, P.1
  • 34
    • 0030736417 scopus 로고    scopus 로고
    • A-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation
    • Barak, L. S., Ferguson, S. S., Zhang, J., Caron, M. G. A-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. J. Biol. Chem. 272, 27497-27500 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 27497-27500
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Caron, M.G.4
  • 35
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield, C. J., Feldman, M. E., Wan, L., Almers, W. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4, 691-698 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 36
    • 66349083804 scopus 로고    scopus 로고
    • Cargomediated regulation of a rapid Rab4-dependent recycling pathway
    • Yudowski, G. A., Puthenveedu, M. A., Henry, A. G., von Zastrow, M. Cargomediated regulation of a rapid Rab4-dependent recycling pathway. Mol. Biol. Cell 20, 2774-2784 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2774-2784
    • Yudowski, G.A.1    Puthenveedu, M.A.2    Henry, A.G.3    Von Zastrow, M.4
  • 37
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., Eliceiri, K. W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 38
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: An open-source platform for biological-image analysis
    • Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676-682 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 676-682
    • Schindelin, J.1


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