메뉴 건너뛰기




Volumn 417, Issue 1, 2009, Pages 287-296

β-Arrestin1 interacts with the G-protein subunits β1γ 2 and promotes β1γ 2-dependent Akt signalling for NF-κB activation

Author keywords

arrestin; Akt; GTP binding protein subunit (G ); Nuclear factor B (NF B)

Indexed keywords

AKT; AKT PHOSPHORYLATION; ARRESTINS; DELETION MUTAGENESIS; G PROTEIN; IN-VITRO; NOVEL FUNCTIONS; NUCLEAR FACTORS; NUCLEAR TRANSLOCATIONS; OVER-EXPRESSION; SMALL INTERFERING RNA; TRANSFECTED CELLS;

EID: 58249088830     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081561     Document Type: Article
Times cited : (46)

References (53)
  • 2
    • 0025352299 scopus 로고
    • β-Arrestin: A protein that regulates β-adrenergic receptor function
    • Lohse, M. J., Benovic, J. L., Codina, J., Caron, M. G. and Lefkowitz, R. J. (1990) β-Arrestin: a protein that regulates β-adrenergic receptor function. Science 248, 1547-1550
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 4
    • 0029057061 scopus 로고
    • Phosphorylation and desensitization of the human β1-adrenergic receptor. Involvement of G protein-coupled receptor kinases and cAMP-dependent protein kinase
    • Freedman, N. J., Liggett, S. B., Drachman, D. E., Pei, G., Caron, M. G. and Lefkowitz, R. J. (1995) Phosphorylation and desensitization of the human β1-adrenergic receptor. Involvement of G protein-coupled receptor kinases and cAMP-dependent protein kinase. J. Biol. Chem. 270, 17953-17961
    • (1995) J. Biol. Chem , vol.270 , pp. 17953-17961
    • Freedman, N.J.1    Liggett, S.B.2    Drachman, D.E.3    Pei, G.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 5
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by β-arrestins
    • Lefkowitz, R. J. and Shenoy, S. K. (2005) Transduction of receptor signals by β-arrestins. Science 308, 512-517
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 9
    • 0034689003 scopus 로고    scopus 로고
    • β-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea, K. A., Zalevsky, J., Thoma, M. S., Dery, O., Mullins, R. D. and Bunnett, N. W. (2000) β-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148, 1267-1281
    • (2000) J. Cell Biol , vol.148 , pp. 1267-1281
    • DeFea, K.A.1    Zalevsky, J.2    Thoma, M.S.3    Dery, O.4    Mullins, R.D.5    Bunnett, N.W.6
  • 10
    • 1342282975 scopus 로고    scopus 로고
    • α-thrombin-mediated phosphatidylinositol 3-kinase activation through release of Gβγ dimers from Gαq and Gαi2
    • Goel, R., Phillips-Mason, P. J., Gardner, A., Raben, D. M. and Baldassare, J. J. (2004) α-thrombin-mediated phosphatidylinositol 3-kinase activation through release of Gβγ dimers from Gαq and Gαi2. J. Biol. Chem. 279, 6701-6710
    • (2004) J. Biol. Chem , vol.279 , pp. 6701-6710
    • Goel, R.1    Phillips-Mason, P.J.2    Gardner, A.3    Raben, D.M.4    Baldassare, J.J.5
  • 11
    • 2942554958 scopus 로고    scopus 로고
    • β-Arrestin inhibits NF-κB activity by means of its interaction with the NF-κB inhibitor IκBα
    • Witherow, D. S., Garrison, T. R., Miller, W. E. and Lefkowitz, R. J. (2004) β-Arrestin inhibits NF-κB activity by means of its interaction with the NF-κB inhibitor IκBα. Proc. Natl. Acad. Sci. U.S.A. 101, 8603-8607
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 8603-8607
    • Witherow, D.S.1    Garrison, T.R.2    Miller, W.E.3    Lefkowitz, R.J.4
  • 12
    • 2342510314 scopus 로고    scopus 로고
    • Identification of β-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-κB pathways
    • Gao, H., Sun, Y., Wu, Y., Luan, B., Wang, Y., Qu, B. and Pei, G. (2004) Identification of β-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-κB pathways. Mol. Cell 14, 303-317
    • (2004) Mol. Cell , vol.14 , pp. 303-317
    • Gao, H.1    Sun, Y.2    Wu, Y.3    Luan, B.4    Wang, Y.5    Qu, B.6    Pei, G.7
  • 14
  • 15
    • 0033961280 scopus 로고    scopus 로고
    • Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB
    • Madrid, L. V., Wang, C. Y., Guttridge, D. C., Schottelius, A. J., Baldwin, Jr, A. S. and Mayo, M. W. (2000) Akt suppresses apoptosis by stimulating the transactivation potential of the RelA/p65 subunit of NF-κB. Mol. Cell. Biol. 20, 1626-1638
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1626-1638
    • Madrid, L.V.1    Wang, C.Y.2    Guttridge, D.C.3    Schottelius, A.J.4    Baldwin Jr, A.S.5    Mayo, M.W.6
  • 16
    • 0028985037 scopus 로고
    • NF-κB and rel proteins in innate immunity
    • Kopp, E. B. and Ghosh, S. (1995) NF-κB and rel proteins in innate immunity. Adv. Immunol. 58, 1-27
    • (1995) Adv. Immunol , vol.58 , pp. 1-27
    • Kopp, E.B.1    Ghosh, S.2
  • 17
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-κB activation pathways and their role in innate and adaptive immunity
    • Bonizzi, G. and Karin, M. (2004) The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends Immunol. 25, 280-288
    • (2004) Trends Immunol , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 18
    • 0029031505 scopus 로고
    • Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway
    • Kravchenko, V. V., Pan, Z., Han, J., Herbert, J. M., Ulevitch, R. J. and Ye, R. D. (1995) Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway. J. Biol. Chem. 270, 14928-14934
    • (1995) J. Biol. Chem , vol.270 , pp. 14928-14934
    • Kravchenko, V.V.1    Pan, Z.2    Han, J.3    Herbert, J.M.4    Ulevitch, R.J.5    Ye, R.D.6
  • 19
    • 0033524913 scopus 로고    scopus 로고
    • Lysophosphatidic acid activates NF-κB in fibroblasts. A requirement for multiple inputs
    • Shahrestanifar, M., Fan, X. and Manning, D. R. (1999) Lysophosphatidic acid activates NF-κB in fibroblasts. A requirement for multiple inputs. J. Biol. Chem. 274, 3828-3833
    • (1999) J. Biol. Chem , vol.274 , pp. 3828-3833
    • Shahrestanifar, M.1    Fan, X.2    Manning, D.R.3
  • 20
    • 0035943649 scopus 로고    scopus 로고
    • PYK2 links Gqα and G13α signaling to NF-κB activation
    • Shi, C. S. and Kehrl, J. H. (2001) PYK2 links Gqα and G13α signaling to NF-κB activation. J. Biol. Chem. 276, 31845-31850
    • (2001) J. Biol. Chem , vol.276 , pp. 31845-31850
    • Shi, C.S.1    Kehrl, J.H.2
  • 21
    • 0035216928 scopus 로고    scopus 로고
    • Regulation of nuclear factor κB activation by G-protein-coupled receptors
    • Ye, R. D. (2001) Regulation of nuclear factor κB activation by G-protein-coupled receptors. J. Leukoc. Biol. 70, 839-848
    • (2001) J. Leukoc. Biol , vol.70 , pp. 839-848
    • Ye, R.D.1
  • 22
    • 0034637556 scopus 로고    scopus 로고
    • Activation of NF-κB by bradykinin through a Gαq- and Gβγ -dependent pathway that involves phosphoinositide 3-kinase and Akt
    • Xie, P., Browning, D. D., Hay, N., Mackman, N. and Ye, R. D. (2000) Activation of NF-κB by bradykinin through a Gαq- and Gβγ -dependent pathway that involves phosphoinositide 3-kinase and Akt. J. Biol. Chem. 275, 24907-24914
    • (2000) J. Biol. Chem , vol.275 , pp. 24907-24914
    • Xie, P.1    Browning, D.D.2    Hay, N.3    Mackman, N.4    Ye, R.D.5
  • 23
    • 0041341922 scopus 로고    scopus 로고
    • Requirement of Gβγ and c-Src in D2 dopamine receptor-mediated nuclear factor-κB activation
    • Yang, M., Zhang, H., Voyno-Yasenetskaya, T. and Ye, R. D. (2003) Requirement of Gβγ and c-Src in D2 dopamine receptor-mediated nuclear factor-κB activation. Mol. Pharmacol. 64, 447-455
    • (2003) Mol. Pharmacol , vol.64 , pp. 447-455
    • Yang, M.1    Zhang, H.2    Voyno-Yasenetskaya, T.3    Ye, R.D.4
  • 24
    • 22744449073 scopus 로고    scopus 로고
    • An Akt/β-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior
    • Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R. and Caron, M. G. (2005) An Akt/β-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior. Cell 122, 261-273
    • (2005) Cell , vol.122 , pp. 261-273
    • Beaulieu, J.M.1    Sotnikova, T.D.2    Marion, S.3    Lefkowitz, R.J.4    Gainetdinov, R.R.5    Caron, M.G.6
  • 25
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano, S. K., Pace, H. C., Kim, Y. M., Brenner, C. and Benovic, J. L. (2002) Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 41, 3321-3328
    • (2002) Biochemistry , vol.41 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.M.3    Brenner, C.4    Benovic, J.L.5
  • 26
    • 0030047481 scopus 로고    scopus 로고
    • Signaling from G protein-coupled receptors to c-Jun kinase involves βγ subunits of heterotrimeric G proteins acting on a Ras and Rac1-dependent pathway
    • Coso, O. A., Teramoto, H., Simonds, W. F. and Gutkind, J. S. (1996) Signaling from G protein-coupled receptors to c-Jun kinase involves βγ subunits of heterotrimeric G proteins acting on a Ras and Rac1-dependent pathway. J. Biol. Chem. 271, 3963-3966
    • (1996) J. Biol. Chem , vol.271 , pp. 3963-3966
    • Coso, O.A.1    Teramoto, H.2    Simonds, W.F.3    Gutkind, J.S.4
  • 27
    • 0035337140 scopus 로고    scopus 로고
    • Gα16 couples chemoattractant receptors to NF-κB activation
    • Yang, M., Sang, H., Rahman, A., Wu, D., Malik, A. B. and Ye, R. D. (2001) Gα16 couples chemoattractant receptors to NF-κB activation. J. Immunol. 166, 6885-6892
    • (2001) J. Immunol , vol.166 , pp. 6885-6892
    • Yang, M.1    Sang, H.2    Rahman, A.3    Wu, D.4    Malik, A.B.5    Ye, R.D.6
  • 28
    • 0035050819 scopus 로고    scopus 로고
    • Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src
    • Yang, M. and Leonard, J. P. (2001) Identification of mouse NMDA receptor subunit NR2A C-terminal tyrosine sites phosphorylated by coexpression with v-Src. J. Neurochem. 77, 580-588.
    • (2001) J. Neurochem , vol.77 , pp. 580-588
    • Yang, M.1    Leonard, J.P.2
  • 29
    • 0030881617 scopus 로고    scopus 로고
    • Ribozyme-mediated suppression of the G protein γ7 subunit suggests a role in hormone regulation of adenylylcyclase activity
    • Wang, Q., Mullah, B., Hansen, C., Asundi, J. and Robishaw, J. D. (1997) Ribozyme-mediated suppression of the G protein γ7 subunit suggests a role in hormone regulation of adenylylcyclase activity. J. Biol. Chem. 272, 26040-26048
    • (1997) J. Biol. Chem , vol.272 , pp. 26040-26048
    • Wang, Q.1    Mullah, B.2    Hansen, C.3    Asundi, J.4    Robishaw, J.D.5
  • 30
    • 0347623204 scopus 로고    scopus 로고
    • Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs)
    • Persengiev, S. P., Zhu, X. and Green, M. R. (2004) Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 10, 12-18
    • (2004) RNA , vol.10 , pp. 12-18
    • Persengiev, S.P.1    Zhu, X.2    Green, M.R.3
  • 31
    • 0033517189 scopus 로고    scopus 로고
    • NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes, O. N., Mayo, L. D., Gustin, J. A., Pfeffer, S. R., Pfeffer, L. M. and Donner, D. B. (1999) NF-κB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature 401, 82-85
    • (1999) Nature , vol.401 , pp. 82-85
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 32
    • 0033517190 scopus 로고    scopus 로고
    • NF-κB is a target of AKT in anti-apoptotic PDGF signalling
    • Romashkova, J. A. and Makarov, S. S. (1999) NF-κB is a target of AKT in anti-apoptotic PDGF signalling. Nature 401, 86-90
    • (1999) Nature , vol.401 , pp. 86-90
    • Romashkova, J.A.1    Makarov, S.S.2
  • 33
    • 0035957951 scopus 로고    scopus 로고
    • Interferon α/β promotes cell survival by activating nuclear factor κB through phosphatidylinositol 3-kinase and Akt
    • Yang, C. H., Murti, A., Pfeffer, S. R., Kim, J. G., Donner, D. B. and Pfeffer, L. M. (2001) Interferon α/β promotes cell survival by activating nuclear factor κB through phosphatidylinositol 3-kinase and Akt. J. Biol. Chem. 276, 13756-13761
    • (2001) J. Biol. Chem , vol.276 , pp. 13756-13761
    • Yang, C.H.1    Murti, A.2    Pfeffer, S.R.3    Kim, J.G.4    Donner, D.B.5    Pfeffer, L.M.6
  • 34
    • 0033537850 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase activity for bradykinin stimulation of NF-κB activation in cultured human epithelial cells
    • Pan, Z. K., Christiansen, S. C., Ptasznik, A. and Zuraw, B. L. (1999) Requirement of phosphatidylinositol 3-kinase activity for bradykinin stimulation of NF-κB activation in cultured human epithelial cells. J. Biol. Chem. 274, 9918-9922
    • (1999) J. Biol. Chem , vol.274 , pp. 9918-9922
    • Pan, Z.K.1    Christiansen, S.C.2    Ptasznik, A.3    Zuraw, B.L.4
  • 35
    • 0036962405 scopus 로고    scopus 로고
    • β-Arrestin 1 couples thrombin to the rapid activation of the Akt pathway
    • Goel, R. and Baldassare, J. J. (2002) β-Arrestin 1 couples thrombin to the rapid activation of the Akt pathway. Ann. N.Y. Acad. Sci. 973, 138-141
    • (2002) Ann. N.Y. Acad. Sci , vol.973 , pp. 138-141
    • Goel, R.1    Baldassare, J.J.2
  • 36
    • 0037166254 scopus 로고    scopus 로고
    • α-thrombin induces rapid and sustained Akt phosphorylation by β-arrestin1-dependent and -independent mechanisms, and only the sustained Akt phosphorylation is essential for G1 phase progression
    • Goel, R., Phillips-Mason, P. J., Raben, D. M. and Baldassare, J. J. (2002) α-thrombin induces rapid and sustained Akt phosphorylation by β-arrestin1-dependent and -independent mechanisms, and only the sustained Akt phosphorylation is essential for G1 phase progression. J. Biol. Chem. 277, 18640-18648
    • (2002) J. Biol. Chem , vol.277 , pp. 18640-18648
    • Goel, R.1    Phillips-Mason, P.J.2    Raben, D.M.3    Baldassare, J.J.4
  • 37
    • 0347695992 scopus 로고    scopus 로고
    • β-arrestin1 mediates insulin-like growth factor 1 (IGF-1) activation of phosphatidylinositol 3-kinase (PI3K) and anti-apoptosis
    • Povsic, T. J., Kohout, T. A. and Lefkowitz, R. J. (2003) β-arrestin1 mediates insulin-like growth factor 1 (IGF-1) activation of phosphatidylinositol 3-kinase (PI3K) and anti-apoptosis. J. Biol. Chem. 278, 51334-51339
    • (2003) J. Biol. Chem , vol.278 , pp. 51334-51339
    • Povsic, T.J.1    Kohout, T.A.2    Lefkowitz, R.J.3
  • 38
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits
    • Stephens, L., Smrcka, A., Cooke, F. T., Jackson, T. R., Sternweis, P. C. and Hawkins, P. T. (1994) A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits. Cell 77, 83-93
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 39
    • 0029059060 scopus 로고
    • Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB
    • Beg, A. A., Sha, W. C., Bronson, R. T., Ghosh, S. and Baltimore, D. (1995) Embryonic lethality and liver degeneration in mice lacking the RelA component of NF-κB. Nature 376, 167-170
    • (1995) Nature , vol.376 , pp. 167-170
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Ghosh, S.4    Baltimore, D.5
  • 40
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • Wang, C. Y., Mayo, M. W. and Baldwin, Jr, A. S. (1996) TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science 274, 784-787
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr, A.S.3
  • 42
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38
    • Madrid, L. V., Mayo, M. W., Reuther, J. Y. and Baldwin, Jr, A. S. (2001) Akt stimulates the transactivation potential of the RelA/p65 subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38. J. Biol. Chem. 276, 18934-18940
    • (2001) J. Biol. Chem , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin Jr, A.S.4
  • 43
    • 2642531082 scopus 로고    scopus 로고
    • Arrestins block G protein-coupled receptor-mediated apoptosis
    • Revankar, C. M., Vines, C. M., Cimino, D. F. and Prossnitz, E. R. (2004) Arrestins block G protein-coupled receptor-mediated apoptosis. J. Biol. Chem. 279, 24578-24584
    • (2004) J. Biol. Chem , vol.279 , pp. 24578-24584
    • Revankar, C.M.1    Vines, C.M.2    Cimino, D.F.3    Prossnitz, E.R.4
  • 44
    • 0034718604 scopus 로고    scopus 로고
    • The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex
    • DeFea, K. A., Vaughn, Z. D., O'Bryan, E. M., Nishijima, D., Dery, O. and Bunnett, N. W. (2000) The proliferative and antiapoptotic effects of substance P are facilitated by formation of a β-arrestin-dependent scaffolding complex. Proc. Natl. Acad. Sci. U.S.A. 97, 11086-11091
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 11086-11091
    • DeFea, K.A.1    Vaughn, Z.D.2    O'Bryan, E.M.3    Nishijima, D.4    Dery, O.5    Bunnett, N.W.6
  • 45
    • 0035966092 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate activates nuclear factor-κB through Edg receptors. Activation through Edg-3 and Edg-5, but not Edg-1, in human embryonic kidney 293 cells
    • Siehler, S., Wang, Y., Fan, X., Windh, R. T. and Manning, D. R. (2001) Sphingosine 1-phosphate activates nuclear factor-κB through Edg receptors. Activation through Edg-3 and Edg-5, but not Edg-1, in human embryonic kidney 293 cells. J. Biol. Chem. 276, 48733-48739
    • (2001) J. Biol. Chem , vol.276 , pp. 48733-48739
    • Siehler, S.1    Wang, Y.2    Fan, X.3    Windh, R.T.4    Manning, D.R.5
  • 48
    • 28344452845 scopus 로고    scopus 로고
    • A nuclear function of β-arrestin1 in GPCR signaling: Regulation of histone acetylation and gene transcription
    • Kang, J., Shi, Y., Xiang, B., Qu, B., Su, W., Zhu, M., Zhang, M., Bao, G., Wang, F., Zhang, X. et al. (2005) A nuclear function of β-arrestin1 in GPCR signaling: regulation of histone acetylation and gene transcription. Cell 123, 833-847
    • (2005) Cell , vol.123 , pp. 833-847
    • Kang, J.1    Shi, Y.2    Xiang, B.3    Qu, B.4    Su, W.5    Zhu, M.6    Zhang, M.7    Bao, G.8    Wang, F.9    Zhang, X.10
  • 49
    • 0035909783 scopus 로고    scopus 로고
    • β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins
    • Chen, W., Hu, L. A., Semenov, M. V., Yanagawa, S., Kikuchi, A., Lefkowitz, R. J. and Miller, W. E. (2001) β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 14889-14894
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14889-14894
    • Chen, W.1    Hu, L.A.2    Semenov, M.V.3    Yanagawa, S.4    Kikuchi, A.5    Lefkowitz, R.J.6    Miller, W.E.7
  • 50
    • 38949163338 scopus 로고    scopus 로고
    • Rapid xenograft tumor progression in β-arrestin1 transgenic mice due to enhanced tumor angiogenesis
    • Zou, L., Yang, R., Chai, J. and Pei, G. (2008) Rapid xenograft tumor progression in β-arrestin1 transgenic mice due to enhanced tumor angiogenesis. FASEB J. 22, 355-364
    • (2008) FASEB J , vol.22 , pp. 355-364
    • Zou, L.1    Yang, R.2    Chai, J.3    Pei, G.4
  • 51
    • 25844459461 scopus 로고    scopus 로고
    • RACK1 binds to a signal transfer region of Gβγ and inhibits phospholipase C β2 activation
    • Chen, S., Lin, F. and Hamm, H. E. (2005) RACK1 binds to a signal transfer region of Gβγ and inhibits phospholipase C β2 activation. J. Biol. Chem. 280, 33445-33452
    • (2005) J. Biol. Chem , vol.280 , pp. 33445-33452
    • Chen, S.1    Lin, F.2    Hamm, H.E.3
  • 53
    • 29244473549 scopus 로고    scopus 로고
    • Gβγ binds histone deacetylase 5 (HDAC5) and inhibits its transcriptional co-repression activity
    • Spiegelberg, B. D. and Hamm, H. E. (2005) Gβγ binds histone deacetylase 5 (HDAC5) and inhibits its transcriptional co-repression activity. J. Biol. Chem. 280, 41769-41776
    • (2005) J. Biol. Chem , vol.280 , pp. 41769-41776
    • Spiegelberg, B.D.1    Hamm, H.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.