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Volumn 69, Issue 8-9, 2004, Pages 523-529

The role of adapter protein Shc in estrogen non-genomic action

Author keywords

Breast cancer cells; ER ; MAP kinase; Shc; Steroid

Indexed keywords

ADAPTOR PROTEIN; ESTRADIOL; ESTROGEN; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; GROWTH FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN SHC;

EID: 3543020345     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2004.05.012     Document Type: Conference Paper
Times cited : (53)

References (41)
  • 1
    • 0032929779 scopus 로고    scopus 로고
    • Rapid actions of estrogens in GH3/B6 pituitary tumor cells via a plasma membrane version of estrogen receptor-alpha
    • Watson C.S., Norfleet A.M., Pappas T.C., Gametchu B. Rapid actions of estrogens in GH3/B6 pituitary tumor cells via a plasma membrane version of estrogen receptor-alpha. Steroids. 64:1999;5-13
    • (1999) Steroids , vol.64 , pp. 5-13
    • Watson, C.S.1    Norfleet, A.M.2    Pappas, T.C.3    Gametchu, B.4
  • 2
    • 0029669930 scopus 로고    scopus 로고
    • Tyrosine kinase/p21ras/MAP-kinase pathway activation by estradiol-receptor complex in MCF-7 cells
    • Migliaccio A., Di Domenico M., Castoria G., de Falco A., Bontempo P., Nola E., et al. Tyrosine kinase/p21ras/MAP-kinase pathway activation by estradiol-receptor complex in MCF-7 cells. EMBO J. 15:1996;1292-1300
    • (1996) EMBO J. , vol.15 , pp. 1292-1300
    • Migliaccio, A.1    Di Domenico, M.2    Castoria, G.3    De Falco, A.4    Bontempo, P.5    Nola, E.6
  • 3
    • 0035881568 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-OH Kinase (PI3K)/AKT2, activated in breast cancer
    • Sun M., Paciga J.E., Feldman R.I., Yuan Z., Coppola D., Lu Y.Y., et al. Phosphatidylinositol-3-OH Kinase (PI3K)/AKT2, activated in breast cancer. Cancer Res. 61:2001;5985-5991
    • (2001) Cancer Res. , vol.61 , pp. 5985-5991
    • Sun, M.1    Paciga, J.E.2    Feldman, R.I.3    Yuan, Z.4    Coppola, D.5    Lu, Y.Y.6
  • 5
    • 0033780783 scopus 로고    scopus 로고
    • Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF
    • Filardo E.J., Quinn J.A., Bland K.I., Frackelton A.R. Jr. Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF. Mol. Endocrinol. 14:2000;1649-1660
    • (2000) Mol. Endocrinol , vol.14 , pp. 1649-1660
    • Filardo, E.J.1    Quinn, J.A.2    Bland, K.I.3    Frackelton Jr., A.R.4
  • 6
    • 17044455693 scopus 로고    scopus 로고
    • Cell-surface estrogen receptors mediate calcium-dependent nitric oxide release in human endothelia
    • Stefano G.B., Prevot V., Beauvillain J.C., Cadet P., Fimiani C., Welters I., et al. Cell-surface estrogen receptors mediate calcium-dependent nitric oxide release in human endothelia. Circulation. 101:2000;1594-1597
    • (2000) Circulation , vol.101 , pp. 1594-1597
    • Stefano, G.B.1    Prevot, V.2    Beauvillain, J.C.3    Cadet, P.4    Fimiani, C.5    Welters, I.6
  • 7
    • 0034659874 scopus 로고    scopus 로고
    • Estradiol-stimulated nitric oxide release in human granulocytes is dependent on intracellular calcium transients: Evidence of a cell surface estrogen receptor
    • Stefano G.B., Cadet P., Breton C., Goumon Y., Prevot V., Dessaint J.P., et al. Estradiol-stimulated nitric oxide release in human granulocytes is dependent on intracellular calcium transients: evidence of a cell surface estrogen receptor. Blood. 95:2000;3951-3958
    • (2000) Blood , vol.95 , pp. 3951-3958
    • Stefano, G.B.1    Cadet, P.2    Breton, C.3    Goumon, Y.4    Prevot, V.5    Dessaint, J.P.6
  • 8
    • 0036137605 scopus 로고    scopus 로고
    • Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation
    • Song R.X., McPherson R.A., Adam L., Bao Y., Shupnik M., Kumar R., et al. Linkage of rapid estrogen action to MAPK activation by ERalpha-Shc association and Shc pathway activation. Mol. Endocrinol. 16:2002;116-127
    • (2002) Mol. Endocrinol. , vol.16 , pp. 116-127
    • Song, R.X.1    McPherson, R.A.2    Adam, L.3    Bao, Y.4    Shupnik, M.5    Kumar, R.6
  • 9
    • 0035831020 scopus 로고    scopus 로고
    • Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: Dissociation from transcriptional activity
    • Kousteni S., Bellido T., Plotkin L.I., O'Brien C.A., Bodenner D.L., Han L., et al. Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell. 104:2001;719-730
    • (2001) Cell , vol.104 , pp. 719-730
    • Kousteni, S.1    Bellido, T.2    Plotkin, L.I.3    O'Brien, C.A.4    Bodenner, D.L.5    Han, L.6
  • 10
    • 0035817721 scopus 로고    scopus 로고
    • Membrane-associated binding sites for estrogen contribute to growth regulation of human breast cancer cells
    • Marquez D.C., Pietras R.J. Membrane-associated binding sites for estrogen contribute to growth regulation of human breast cancer cells. Oncogene. 20:2001;5420-5430
    • (2001) Oncogene , vol.20 , pp. 5420-5430
    • Marquez, D.C.1    Pietras, R.J.2
  • 11
    • 0022454520 scopus 로고
    • Evidence for a specific estradiol binding site on rat pituitary membranes
    • Bression D., Michard M., Le Dafniet M., Pagesy P., Peillon F. Evidence for a specific estradiol binding site on rat pituitary membranes. Endocrinology. 119:1986;1048-1051
    • (1986) Endocrinology , vol.119 , pp. 1048-1051
    • Bression, D.1    Michard, M.2    Le Dafniet, M.3    Pagesy, P.4    Peillon, F.5
  • 12
    • 0028316126 scopus 로고
    • Specific binding of estrogen to osteoclast surfaces
    • Brubaker K.D., Gay C.V. Specific binding of estrogen to osteoclast surfaces. Biochem. Biophys. Res. Commun. 200:1994;899-907
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 899-907
    • Brubaker, K.D.1    Gay, C.V.2
  • 13
    • 0033985036 scopus 로고    scopus 로고
    • Antibodies to the estrogen receptor-alpha modulate rapid prolactin release from rat pituitary tumor cells through plasma membrane estrogen receptors
    • Norfleet A.M., Clarke C.H., Gametchu B., Watson C.S. Antibodies to the estrogen receptor-alpha modulate rapid prolactin release from rat pituitary tumor cells through plasma membrane estrogen receptors. FASEB J. 14:2000;157-165
    • (2000) FASEB J. , vol.14 , pp. 157-165
    • Norfleet, A.M.1    Clarke, C.H.2    Gametchu, B.3    Watson, C.S.4
  • 15
    • 0033732896 scopus 로고    scopus 로고
    • Plasma membrane estrogen receptors signal to antiapoptosis in breast cancer
    • Razandi M., Pedram A., Levin E.R. Plasma membrane estrogen receptors signal to antiapoptosis in breast cancer. Mol. Endocrinol. 14:2000;1434-1447
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1434-1447
    • Razandi, M.1    Pedram, A.2    Levin, E.R.3
  • 16
    • 17944375553 scopus 로고    scopus 로고
    • PI3-kinase in concert with Src promotes the S-phase entry of oestradiol-stimulated MCF-7 cells
    • Castoria G., Migliaccio A., Bilancio A., Di Domenico M., de Falco A., Lombardi M., et al. PI3-kinase in concert with Src promotes the S-phase entry of oestradiol-stimulated MCF-7 cells. EMBO J. 20:2001;6050-6059
    • (2001) EMBO J. , vol.20 , pp. 6050-6059
    • Castoria, G.1    Migliaccio, A.2    Bilancio, A.3    Di Domenico, M.4    De Falco, A.5    Lombardi, M.6
  • 18
    • 0026713869 scopus 로고
    • Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors
    • Ylikomi T., Bocquel M.T., Berry M., Gronemeyer H., Chambon P. Cooperation of proto-signals for nuclear accumulation of estrogen and progesterone receptors. EMBO J. 11:1992;3681-3694
    • (1992) EMBO J. , vol.11 , pp. 3681-3694
    • Ylikomi, T.1    Bocquel, M.T.2    Berry, M.3    Gronemeyer, H.4    Chambon, P.5
  • 19
    • 0030071445 scopus 로고    scopus 로고
    • Tripartite steroid hormone receptor pharmacology: Interaction with multiple effector sites as a basis for the cell- and promoter-specific action of these hormones
    • Katzenellenbogen J.A., O'Malley B.W., Katzenellenbogen B.S. Tripartite steroid hormone receptor pharmacology: interaction with multiple effector sites as a basis for the cell- and promoter-specific action of these hormones. Mol. Endocrinol. 10:1996;119-131
    • (1996) Mol. Endocrinol. , vol.10 , pp. 119-131
    • Katzenellenbogen, J.A.1    O'Malley, B.W.2    Katzenellenbogen, B.S.3
  • 20
    • 3542998936 scopus 로고    scopus 로고
    • The role of adapter proteins in ER alpha membrane association and function
    • Watson CS, editor. Boston, Dordrecht, London: Kluwer Academic Publishers;
    • Song RX, Kumar R. The role of adapter proteins in ER alpha membrane association and function. In: Watson CS, editor. The identities of membrane steroid receptors. Boston, Dordrecht, London: Kluwer Academic Publishers; 2003. p. 67-76.
    • (2003) The Identities of Membrane Steroid Receptors , pp. 67-76
    • Song, R.X.1    Kumar, R.2
  • 21
    • 0034727094 scopus 로고    scopus 로고
    • Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
    • Simoncini T., Hafezi-Moghadam A., Brazil D.P., Ley K., Chin W.W., Liao J.K. Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase. Nature. 407:2000;538-541
    • (2000) Nature , vol.407 , pp. 538-541
    • Simoncini, T.1    Hafezi-Moghadam, A.2    Brazil, D.P.3    Ley, K.4    Chin, W.W.5    Liao, J.K.6
  • 22
    • 0033581704 scopus 로고    scopus 로고
    • The p66shc adaptor protein controls oxidative stress response and life span in mammals
    • Migliaccio E., Giorgio M., Mele S., Pelicci G., Reboldi P., Pandolfi P.P., et al. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature. 402:1999;309-313
    • (1999) Nature , vol.402 , pp. 309-313
    • Migliaccio, E.1    Giorgio, M.2    Mele, S.3    Pelicci, G.4    Reboldi, P.5    Pandolfi, P.P.6
  • 23
    • 0035474473 scopus 로고    scopus 로고
    • Signaling via Shc family adapter proteins
    • Ravichandran K.S. Signaling via Shc family adapter proteins. Oncogene. 20:2001;6322-6330
    • (2001) Oncogene , vol.20 , pp. 6322-6330
    • Ravichandran, K.S.1
  • 26
    • 0026678172 scopus 로고
    • Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock M., McGlade J., Mbamalu G., Pelicci G., Daly R., Li W., et al. Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature. 360:1992;689-692
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1    McGlade, J.2    Mbamalu, G.3    Pelicci, G.4    Daly, R.5    Li, W.6
  • 27
    • 0034464905 scopus 로고    scopus 로고
    • The critical role of Shc in insulin-like growth factor-I-mediated mitogenesis and differentiation in 3T3-L1 preadipocytes
    • Boney C.M., Gruppuso P.A., Faris R.A., Frackelton A.R. Jr. The critical role of Shc in insulin-like growth factor-I-mediated mitogenesis and differentiation in 3T3-L1 preadipocytes. Mol. Endocrinol. 14:2000;805-813
    • (2000) Mol. Endocrinol. , vol.14 , pp. 805-813
    • Boney, C.M.1    Gruppuso, P.A.2    Faris, R.A.3    Frackelton Jr., A.R.4
  • 28
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard S.R., Till J.H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69:2000;373-398
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 29
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein tyrosine kinases
    • Superti-Furga G., Courtneidge S.A. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays. 17:1995;321-330
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 30
    • 0028983318 scopus 로고
    • Regulation of the Src protein tyrosine kinase
    • Superti-Furga G. Regulation of the Src protein tyrosine kinase. FEBS Lett. 369:1995;62-66
    • (1995) FEBS Lett. , vol.369 , pp. 62-66
    • Superti-Furga, G.1
  • 31
    • 0033604577 scopus 로고    scopus 로고
    • Signaling by distinct classes of phosphoinositide 3-kinases
    • Vanhaesebroeck B., Waterfield M.D. Signaling by distinct classes of phosphoinositide 3-kinases. Exp. Cell Res. 253:1999;239-254
    • (1999) Exp. Cell Res. , vol.253 , pp. 239-254
    • Vanhaesebroeck, B.1    Waterfield, M.D.2
  • 33
    • 0029085477 scopus 로고
    • Interaction of p85 subunit of PI 3-kinase with insulin and IGF-1 receptors analysed by using the two-hybrid system
    • Lamothe B., Bucchini D., Jami J., Joshi R.L. Interaction of p85 subunit of PI 3-kinase with insulin and IGF-1 receptors analysed by using the two-hybrid system. FEBS Lett. 373:1995;51-55
    • (1995) FEBS Lett. , vol.373 , pp. 51-55
    • Lamothe, B.1    Bucchini, D.2    Jami, J.3    Joshi, R.L.4
  • 34
    • 0028142280 scopus 로고
    • Insulin-like growth factor-1-mediated association of p85 phosphatidylinositol 3-kinase with pp 185: Requirement of SH2 domains for in vivo interaction
    • Altschuler D., Yamamoto K., Lapetina E.G. Insulin-like growth factor-1-mediated association of p85 phosphatidylinositol 3-kinase with pp 185: requirement of SH2 domains for in vivo interaction. Mol. Endocrinol. 8:1994;1139-1146
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1139-1146
    • Altschuler, D.1    Yamamoto, K.2    Lapetina, E.G.3
  • 35
    • 0026753401 scopus 로고
    • Association of phosphorylated insulin-like growth factor-I receptor with the SH2 domains of phosphatidylinositol 3-kinase p85
    • Yamamoto K., Altschuler D., Wood E., Horlick K., Jacobs S., Lapetina E.G. Association of phosphorylated insulin-like growth factor-I receptor with the SH2 domains of phosphatidylinositol 3-kinase p85. J. Biol. Chem. 267:1992;11337-11343
    • (1992) J. Biol. Chem. , vol.267 , pp. 11337-11343
    • Yamamoto, K.1    Altschuler, D.2    Wood, E.3    Horlick, K.4    Jacobs, S.5    Lapetina, E.G.6
  • 37
    • 0034841661 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling in breast cancer: How big a role might it play?
    • Fry M.J. Phosphoinositide 3-kinase signalling in breast cancer: how big a role might it play? Breast Cancer Res. 3:2001;304-312
    • (2001) Breast Cancer Res. , vol.3 , pp. 304-312
    • Fry, M.J.1
  • 38
    • 0032036584 scopus 로고    scopus 로고
    • Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor
    • Migliaccio A., Piccolo D., Castoria G., Di Domenico M., Bilancio A., Lombardi M., et al. Activation of the Src/p21ras/Erk pathway by progesterone receptor via cross-talk with estrogen receptor. EMBO J. 17:1998;2008-2018
    • (1998) EMBO J. , vol.17 , pp. 2008-2018
    • Migliaccio, A.1    Piccolo, D.2    Castoria, G.3    Di Domenico, M.4    Bilancio, A.5    Lombardi, M.6
  • 39
    • 0035206637 scopus 로고    scopus 로고
    • Estradiol (E2) elicits SRC phosphorylation in the mouse neocortex: The initial event in E2 activation of the MAPK cascade?
    • Nethrapalli I.S., Singh M., Guan X., Guo Q., Lubahn D.B., Korach K.S., et al. Estradiol (E2) elicits SRC phosphorylation in the mouse neocortex: the initial event in E2 activation of the MAPK cascade? Endocrinology. 142:2001;5145-5148
    • (2001) Endocrinology , vol.142 , pp. 5145-5148
    • Nethrapalli, I.S.1    Singh, M.2    Guan, X.3    Guo, Q.4    Lubahn, D.B.5    Korach, K.S.6
  • 40
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases
    • Boonyaratanakornkit V., Scott M.P., Ribon V., Sherman L., Anderson S.M., Maller J.L., et al. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol. Cell. 8:2001;269-280
    • (2001) Mol. Cell , vol.8 , pp. 269-280
    • Boonyaratanakornkit, V.1    Scott, M.P.2    Ribon, V.3    Sherman, L.4    Anderson, S.M.5    Maller, J.L.6
  • 41
    • 0032561206 scopus 로고    scopus 로고
    • Heregulin regulates cytoskeletal reorganization and cell migration through the p21-activated kinase-1 via phosphatidylinositol-3 kinase
    • Adam L., Vadlamudi R., Kondapaka S.B., Chernoff J., Mendelsohn J., Kumar R. Heregulin regulates cytoskeletal reorganization and cell migration through the p21-activated kinase-1 via phosphatidylinositol-3 kinase. J. Biol. Chem. 273:1998;28238-28246
    • (1998) J. Biol. Chem. , vol.273 , pp. 28238-28246
    • Adam, L.1    Vadlamudi, R.2    Kondapaka, S.B.3    Chernoff, J.4    Mendelsohn, J.5    Kumar, R.6


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