메뉴 건너뛰기




Volumn 16, Issue 1, 2005, Pages 231-237

Palmitoylation-dependent estrogen receptor α membrane localization: Regulation by 17β-estradiol

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CYCLIN D1; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; PROTEIN KINASE B;

EID: 11144332004     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-07-0547     Document Type: Article
Times cited : (408)

References (47)
  • 2
    • 14744283561 scopus 로고    scopus 로고
    • Survival versus apoptotic 17β-estradiol effect: Role of ERα and ERβ activated non-genomic signalling
    • Published online
    • Acconcia, F., Totta, P., Ogawa, S., Cardillo, I., Inoue, S., Leone, S., Trentalance, A., Muramatsu, M., and Marino, M. (2004a). Survival versus apoptotic 17β-estradiol effect: role of ERα and ERβ activated non-genomic signalling. J. Cell. Physiol. Published online at www.interscience.wiley.com/DOI10.1002/ 5CP.20219.
    • (2004) J. Cell. Physiol.
    • Acconcia, F.1    Totta, P.2    Ogawa, S.3    Cardillo, I.4    Inoue, S.5    Leone, S.6    Trentalance, A.7    Muramatsu, M.8    Marino, M.9
  • 3
    • 1442274918 scopus 로고    scopus 로고
    • Membrane-associated estrogen receptor and caveolin-1 are present in central nervous system myelin and oligodendrocyte plasma membranes
    • Arvanitis, D. N., Wang, H., Bagshaw, R. D., Callahan, J. W., and Boggs, J. M. (2004). Membrane-associated estrogen receptor and caveolin-1 are present in central nervous system myelin and oligodendrocyte plasma membranes. J. Neurosci. Res. 75, 603-613.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 603-613
    • Arvanitis, D.N.1    Wang, H.2    Bagshaw, R.D.3    Callahan, J.W.4    Boggs, J.M.5
  • 4
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M. J., and Marsh, M. (2003). The on-off story of protein palmitoylation. Trends Cell Biol. 13, 32-42.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 772, 248-254.
    • (1976) Anal. Biochem. , vol.772 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0036230688 scopus 로고    scopus 로고
    • Rapid activation of endothelial NO synthase by estrogen: Evidence for a steroid receptor fast-action complex (SRFC) in caveolae
    • Chambliss, K. L., and Shaul, P. W. (2002). Rapid activation of endothelial NO synthase by estrogen: evidence for a steroid receptor fast-action complex (SRFC) in caveolae. Steroids 67, 413-419.
    • (2002) Steroids , vol.67 , pp. 413-419
    • Chambliss, K.L.1    Shaul, P.W.2
  • 11
    • 0035487829 scopus 로고    scopus 로고
    • Intracellular signaling pathways: Nongenomic actions of estrogens and ligand-independent activation of estrogen receptors
    • Coleman, K. M., and Smith, C. L. (2001). Intracellular signaling pathways: nongenomic actions of estrogens and ligand-independent activation of estrogen receptors. Front. Biosci. 6, D1379-D1391.
    • (2001) Front. Biosci. , vol.6
    • Coleman, K.M.1    Smith, C.L.2
  • 12
    • 0037377558 scopus 로고    scopus 로고
    • Epitope-dependent localization of estrogen receptor-α, but not -β, in en face arterial endothelium
    • Dan, P., Cheung, J.C., Scriven, D. R., and Moore, E. D. (2003). Epitope-dependent localization of estrogen receptor-α, but not -β, in en face arterial endothelium. Am. J. Physiol. 284, H1295-H1306.
    • (2003) Am. J. Physiol. , vol.284
    • Dan, P.1    Cheung, J.C.2    Scriven, D.R.3    Moore, E.D.4
  • 13
    • 0842334814 scopus 로고    scopus 로고
    • Characterization of a membrane-associated estrogen receptor in a rat hypothalamic cell line (D12)
    • Deecher, D. C., Swiggard, P., Frail, D. E., and O'Connor, L. T. (2003). Characterization of a membrane-associated estrogen receptor in a rat hypothalamic cell line (D12). Endocrine 22, 211-223.
    • (2003) Endocrine , vol.22 , pp. 211-223
    • Deecher, D.C.1    Swiggard, P.2    Frail, D.E.3    O'Connor, L.T.4
  • 14
    • 3042843668 scopus 로고    scopus 로고
    • Estradiol abrogates apoptosis in breast cancer cells through inactivation of BAD: Ras dependent non-genomic pathways requiring signaling through ERK and AKT
    • Fernando, R. I., and Wimalasena, J. (2004). Estradiol abrogates apoptosis in breast cancer cells through inactivation of BAD: Ras dependent non-genomic pathways requiring signaling through ERK and AKT. Mol. Biol. Cell 15, 3266-3284.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3266-3284
    • Fernando, R.I.1    Wimalasena, J.2
  • 15
    • 0036854304 scopus 로고    scopus 로고
    • Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: Implications for epidermal growth factor signalling
    • Han, J. M., Kim, Y., Lee, J. S., Lee, C. S., Lee, B. D., Ohba, M., Kuroki, T., Suh, P.-G., and Ryu, S. H. (2002). Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signalling. Mol. Biol. Cell 13, 3976-3988.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3976-3988
    • Han, J.M.1    Kim, Y.2    Lee, J.S.3    Lee, C.S.4    Lee, B.D.5    Ohba, M.6    Kuroki, T.7    Suh, P.-G.8    Ryu, S.H.9
  • 16
    • 0029979932 scopus 로고    scopus 로고
    • Carboxymethylation of the human estrogen receptor ligand-binding domain-estradiol complex: HPLC/ESMS peptide mapping shows that cysteine 447 does not react with iodoacetic acid
    • Hegy, G. B., Shackleton, C. H., Carlquist, M., Bonn, T., Engstrom, O., Sjoholm, P., and Witkowska, H. E. (1996). Carboxymethylation of the human estrogen receptor ligand-binding domain-estradiol complex: HPLC/ESMS peptide mapping shows that cysteine 447 does not react with iodoacetic acid. Steroids 61, 367-373.
    • (1996) Steroids , vol.61 , pp. 367-373
    • Hegy, G.B.1    Shackleton, C.H.2    Carlquist, M.3    Bonn, T.4    Engstrom, O.5    Sjoholm, P.6    Witkowska, H.E.7
  • 18
    • 0036795423 scopus 로고    scopus 로고
    • An estrogen receptor ERα deoxyribonucleic acid-binding domain knock-in mutation provides evidence for nonclassical ER pathway signaling in vivo
    • Jakacka, M., Ito, M., Martinson, F., Ishikawa, T., Lee, E. J., and Jameson, J. L. (2002). An estrogen receptor ERα deoxyribonucleic acid-binding domain knock-in mutation provides evidence for nonclassical ER pathway signaling in vivo. Mol. Endocrinol. 16, 2188-2201.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 2188-2201
    • Jakacka, M.1    Ito, M.2    Martinson, F.3    Ishikawa, T.4    Lee, E.J.5    Jameson, J.L.6
  • 20
    • 0035347192 scopus 로고    scopus 로고
    • Rapid actions of plasma membrane estrogen receptors
    • Kelly, M. J., and Levin, E. R. (2001). Rapid actions of plasma membrane estrogen receptors. Trends Endocrinol. Metab. 12, 152-156.
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 152-156
    • Kelly, M.J.1    Levin, E.R.2
  • 21
    • 0035831020 scopus 로고    scopus 로고
    • Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: Dissociation from transcriptional activity
    • Kousteni, S., et al. (2001). Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell 104, 719-790.
    • (2001) Cell , vol.104 , pp. 719-790
    • Kousteni, S.1
  • 22
    • 0034802322 scopus 로고    scopus 로고
    • Cell localization, physiology, and nongenomic actions of estrogen receptors
    • Levin, E. R. (2001). Cell localization, physiology, and nongenomic actions of estrogen receptors. J. Appl. Physiol. 91, 1860-1867.
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1860-1867
    • Levin, E.R.1
  • 23
    • 0037446887 scopus 로고    scopus 로고
    • Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
    • Li, L., Haynes, M. P., and Bender, J. R. (2003). Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proc. Natl. Acad. Sci. USA 100, 4807-4812.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4807-4812
    • Li, L.1    Haynes, M.P.2    Bender, J.R.3
  • 24
    • 0034014355 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase and phosphatidylinositol 3-kinase activity in MCF-7 cells prevents estrogen-induced mitogenesis
    • Lobenhofer, E. K., Huper, G., Iglehart, J. D., and Marks, J. R. (2000). Inhibition of mitogen-activated protein kinase and phosphatidylinositol 3-kinase activity in MCF-7 cells prevents estrogen-induced mitogenesis. Cell Growth Differ. 11, 99-110.
    • (2000) Cell Growth Differ. , vol.11 , pp. 99-110
    • Lobenhofer, E.K.1    Huper, G.2    Iglehart, J.D.3    Marks, J.R.4
  • 25
    • 0037377019 scopus 로고    scopus 로고
    • Selective plasma membrane permeabilization by freeze-thawing and immunofluorescence epitope access to determine the topology of intracellular membrane proteins
    • Mardones, G., and Gonzalez, A. (2003). Selective plasma membrane permeabilization by freeze-thawing and immunofluorescence epitope access to determine the topology of intracellular membrane proteins. J. Immunol. Methods 275, 169-177.
    • (2003) J. Immunol. Methods , vol.275 , pp. 169-177
    • Mardones, G.1    Gonzalez, A.2
  • 27
    • 0034941591 scopus 로고    scopus 로고
    • β-estradiol stimulation of DNA synthesis requires different PKC isoforms in HepG2 and MCF7 cells
    • Marino, M., Distefano, E., Pallottini, V., Caporali, S., Ceracchi, G., and Trentalance, A. (2001a). β-Estradiol stimulation of DNA synthesis requires different PKC isoforms in HepG2 and MCF7 cells. J. Cell Physiol. 188, 170-177.
    • (2001) J. Cell Physiol. , vol.188 , pp. 170-177
    • Marino, M.1    Distefano, E.2    Pallottini, V.3    Caporali, S.4    Ceracchi, G.5    Trentalance, A.6
  • 30
    • 0037699972 scopus 로고    scopus 로고
    • Biphasic estradiol-induced AKT-phosphorylation is modulated by PTEN via MAP kinase in HepG2 cells
    • Marino, M., Acconcia, F., and Trentalance, A. (2003). Biphasic estradiol-induced AKT-phosphorylation is modulated by PTEN via MAP kinase in HepG2 cells. Mol. Biol. Cell 14, 2583-2591.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2583-2591
    • Marino, M.1    Acconcia, F.2    Trentalance, A.3
  • 32
    • 0028021514 scopus 로고
    • Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution
    • Neff, S., Sadowski, C., and Miksicek, R. J. (1994). Mutational analysis of cysteine residues within the hormone-binding domain of the human estrogen receptor identifies mutants that are defective in both DNA-binding and subcellular distribution. Mol. Endocrinol. 8, 1215-1223.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1215-1223
    • Neff, S.1    Sadowski, C.2    Miksicek, R.J.3
  • 33
    • 0033304691 scopus 로고    scopus 로고
    • Estrogen receptor-α detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme-linked immunocytochemistry
    • Norfleet, A. M., Thomas, M. L., Gametchu, B., and Watson, C. S. (1999). Estrogen receptor-α detected on the plasma membrane of aldehyde-fixed GH3/B6/F10 rat pituitary tumor cells by enzyme-linked immunocytochemistry. Endocrinology 140, 3805-3814.
    • (1999) Endocrinology , vol.140 , pp. 3805-3814
    • Norfleet, A.M.1    Thomas, M.L.2    Gametchu, B.3    Watson, C.S.4
  • 34
    • 0028925081 scopus 로고
    • Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding
    • Pappas, T. C., Gametchu, B., and Watson, C. S. (1995). Membrane estrogen receptors identified by multiple antibody labeling and impeded-ligand binding. FASEB J. 9, 404-410.
    • (1995) FASEB J. , vol.9 , pp. 404-410
    • Pappas, T.C.1    Gametchu, B.2    Watson, C.S.3
  • 35
    • 0001548401 scopus 로고    scopus 로고
    • Cell membrane and nuclear estrogen receptors (ERs) originate from a single transcript: Studies of ERα and ERβ expressed in Chinese hamster ovary cells
    • Razandi, M., Pedram, A., Greene, G. L., and Levin, E. R. (1999). Cell membrane and nuclear estrogen receptors (ERs) originate from a single transcript: studies of ERα and ERβ expressed in Chinese hamster ovary cells. Mol. Endocrinol. 13, 307-319.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 307-319
    • Razandi, M.1    Pedram, A.2    Greene, G.L.3    Levin, E.R.4
  • 36
    • 0033732896 scopus 로고    scopus 로고
    • Plasma membrane estrogen receptors signal to antiapoptosis in breast cancer
    • Razandi, M., Pedram, A., and Levin, E. R. (2000). Plasma membrane estrogen receptors signal to antiapoptosis in breast cancer. Mol. Endocrinol. 14, 1434-1447.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1434-1447
    • Razandi, M.1    Pedram, A.2    Levin, E.R.3
  • 37
    • 0036139164 scopus 로고    scopus 로고
    • ERs associate with and regulate the production of caveolin: Implications for signaling and cellular actions
    • Razandi, M., Oh, P., Pedram, A., Schnitzer, J., and Levin, E. R. (2002). ERs associate with and regulate the production of caveolin: implications for signaling and cellular actions. Mol. Endocrinol. 16, 100-115.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 100-115
    • Razandi, M.1    Oh, P.2    Pedram, A.3    Schnitzer, J.4    Levin, E.R.5
  • 38
    • 0037371627 scopus 로고    scopus 로고
    • Identification of a structural determinant necessary for the localization and function of estrogen receptor α at the plasma membrane
    • Razandi, M., Alton, G., Pedram, A., Ghonshani, S., Webb, P., and Levin, E. R. (2003). Identification of a structural determinant necessary for the localization and function of estrogen receptor α at the plasma membrane. Mol. Cell. Biol. 23, 1633-1646.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1633-1646
    • Razandi, M.1    Alton, G.2    Pedram, A.3    Ghonshani, S.4    Webb, P.5    Levin, E.R.6
  • 39
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid, G., Hubner, M. R., Metivier, R., Brand, H., Denger, S., Manu, D., Beaudouin, J., Ellenberg, J., and Cannon, F. (2003). Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11, 695-707.
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Cannon, F.9
  • 40
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 41
    • 0036188982 scopus 로고    scopus 로고
    • A nonclassical estrogen membrane receptor triggers rapid differential actions in the endocrine pancreas
    • Ropero, A. B., Soria, B., and Nadal, A. (2002). A nonclassical estrogen membrane receptor triggers rapid differential actions in the endocrine pancreas. Mol. Endocrinol. 16, 497-505.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 497-505
    • Ropero, A.B.1    Soria, B.2    Nadal, A.3
  • 42
    • 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., and Liao, J. K. (2000). Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase. Nature 407, 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
  • 43
    • 0036137605 scopus 로고    scopus 로고
    • Linkage of rapid estrogen action to MAPK activation by ERα-Shc association and Shc pathway activation
    • Song, R. X., McPherson, R. A., Adam, L., Bao, Y., Shupnik, M., Kumar, R., and Santen, R. J. (2002). Linkage of rapid estrogen action to MAPK activation by ERα-Shc association and Shc pathway activation. Mol. Endocrinol. 16, 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    Santen, R.J.7
  • 44
    • 1242341918 scopus 로고    scopus 로고
    • The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane
    • Song, R. X., Barnes, C. J., Zhang, Z., Bao, Y., Kumar, R., and Santen, R. J. (2004). The role of Shc and insulin-like growth factor 1 receptor in mediating the translocation of estrogen receptor α to the plasma membrane. Proc. Natl. Acad. Sci. USA 101, 2076-2081.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2076-2081
    • Song, R.X.1    Barnes, C.J.2    Zhang, Z.3    Bao, Y.4    Kumar, R.5    Santen, R.J.6
  • 46
    • 0038343919 scopus 로고    scopus 로고
    • Characterization of human palmitoyl-acyl transferase activity using peptides that mimic distinct palmitoylation motifs
    • Varner, A. S., Ducker, C. E., Xia, Z., Zhuang, Y., De Vos, M. L., and Smith, C. D. (2003). Characterization of human palmitoyl-acyl transferase activity using peptides that mimic distinct palmitoylation motifs. Biochem. J. 373, 91-99.
    • (2003) Biochem. J. , vol.373 , pp. 91-99
    • Varner, A.S.1    Ducker, C.E.2    Xia, Z.3    Zhuang, Y.4    De Vos, M.L.5    Smith, C.D.6
  • 47
    • 0035089767 scopus 로고    scopus 로고
    • Neuroprotective effects of estrogen-new insights into mechanisms of action
    • Wise, P. M., Dubal, D. B., Wilson, M. E., Rau, S. W., and Bottner, M. (2001). Neuroprotective effects of estrogen-new insights into mechanisms of action. Endocrinology 142, 969-973.
    • (2001) Endocrinology , vol.142 , pp. 969-973
    • Wise, P.M.1    Dubal, D.B.2    Wilson, M.E.3    Rau, S.W.4    Bottner, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.