메뉴 건너뛰기




Volumn 28, Issue 1, 2009, Pages 67-71

PKA-Mediated stabilization of FoxH1 negatively regulates ERα activity

Author keywords

Estrogen receptor ; FoxH1; Protein kinase A; Protein stability

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; FORKHEAD TRANSCRIPTION FACTOR; FORSKOLIN; PROTEIN FOXH1; UNCLASSIFIED DRUG;

EID: 69849083757     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10059-009-0099-7     Document Type: Article
Times cited : (11)

References (28)
  • 1
    • 33846568011 scopus 로고    scopus 로고
    • Protein kinase A exhibits selective modulation of estradiol-dependent transcription in breast cancer cells that is associated with decreased ligand binding, altered estrogen receptor α promoter interaction, and changes in receptor phosphorylation
    • Al-Dhaheri, M.H., and Rowan, B.G. (2007). Protein kinase A exhibits selective modulation of estradiol-dependent transcription in breast cancer cells that is associated with decreased ligand binding, altered estrogen receptor α promoter interaction, and changes in receptor phosphorylation. Mol. Endocrinol. 21, 439-456.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 439-456
    • Al-Dhaheri, M.H.1    Rowan, B.G.2
  • 2
    • 0028833473 scopus 로고
    • Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro
    • Arnold, S.F., Obourn, J.D., Jaffe, H., and Notides, A.C. (1995). Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol. Endocrinol. 9, 24-33.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 24-33
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3    Notides, A.C.4
  • 4
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization
    • Chen, D., Pace, P.E., Coombes, R.C., and Ali, S. (1999). Phosphorylation of human estrogen receptor α by protein kinase A regulates dimerization. Mol. Cell. Biol. 19, 1002-1015.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1002-1015
    • Chen, D.1    Pace, P.E.2    Coombes, R.C.3    Ali, S.4
  • 6
    • 0027509872 scopus 로고
    • Synergistic activation of estrogen receptor-mediated transcription by estradiol and protein kinase activators
    • Cho, H., and Katzenellenbogen, B.S. (1993). Synergistic activation of estrogen receptor-mediated transcription by estradiol and protein kinase activators. Mol. Endocrinol. 7, 441-452.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 441-452
    • Cho, H.1    Katzenellenbogen, B.S.2
  • 7
    • 10844286471 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor α blocks its acetylation and regulates estrogen sensitivity
    • Cui, Y., Zhang, M., Pestell, R., Curran, E.M., Welshons, W.V., and Fuqua, S.A. (2004). Phosphorylation of estrogen receptor α blocks its acetylation and regulates estrogen sensitivity. Cancer Res. 64, 9199-9208.
    • (2004) Cancer Res. , vol.64 , pp. 9199-9208
    • Cui, Y.1    Zhang, M.2    Pestell, R.3    Curran, E.M.4    Welshons, W.V.5    Fuqua, S.A.6
  • 8
    • 0035134504 scopus 로고    scopus 로고
    • Potentiation of estrogen receptor activation function 1 (AF-1) by Src/ JNK through a serine 118-independent pathway
    • Feng, W., Webb, P., Nguyen, P., Liu, X., Li, J., Karin, M., and Kushner, P.J. (2001). Potentiation of estrogen receptor activation function 1 (AF-1) by Src/JNK through a serine 118-independent pathway. Mol. Endocrinol. 15, 32-45.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 32-45
    • Feng, W.1    Webb, P.2    Nguyen, P.3    Liu, X.4    Li, J.5    Karin, M.6    Kushner, P.J.7
  • 9
    • 69849105847 scopus 로고    scopus 로고
    • Tectoridin, a poor ligand of estrogen receptor alpha, exerts its estrogenic effects via an ERK-dependent pathway
    • Kang, K., Lee, S.B., Jung, S.H., Cha, K.H., Park, W.D., Sohn, Y.C., and Nho, C.W. (2009). Tectoridin, a poor ligand of estrogen receptor alpha, exerts its estrogenic effects via an ERK-dependent pathway. Mol. Cells 27, 351-357.
    • (2009) Mol. Cells , vol.27 , pp. 351-357
    • Kang, K.1    Lee, S.B.2    Jung, S.H.3    Cha, K.H.4    Park, W.D.5    Sohn, Y.C.6    Nho, C.W.7
  • 12
    • 0037211754 scopus 로고    scopus 로고
    • Estrogen receptor phosphorylation
    • Lannigan, D.A. (2003). Estrogen receptor phosphorylation. Steroids 68, 1-9.
    • (2003) Steroids , vol.68 , pp. 1-9
    • Lannigan, D.A.1
  • 13
    • 0036318571 scopus 로고    scopus 로고
    • Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation
    • Lee, H., and Bai, W. (2002). Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol. Cell. Biol. 22, 5835-5845.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5835-5845
    • Lee, H.1    Bai, W.2
  • 14
    • 0035811531 scopus 로고    scopus 로고
    • Interaction of estrogen receptors α and β with estrogen response elements
    • Loven, M.A., Wood, J.R., and Nardulli, A.M. (2001). Interaction of estrogen receptors α and β with estrogen response elements. Mol. Cell. Endocrinol. 181, 151-163.
    • (2001) Mol. Cell. Endocrinol. , vol.181 , pp. 151-163
    • Loven, M.A.1    Wood, J.R.2    Nardulli, A.M.3
  • 15
    • 33646562542 scopus 로고    scopus 로고
    • The logic of TGFβ signaling
    • Massagué, J., and Gomis, R.R. (2006). The logic of TGFβ signaling. FEBS Lett. 580, 2811-2820.
    • (2006) FEBS Lett. , vol.580 , pp. 2811-2820
    • Massagué, J.1    Gomis, R.R.2
  • 16
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna, N.J., Lanz, R.B., and O'Malley, B.W. (1999). Nuclear receptor coregulators: Cellular and molecular biology. Endocrine Rev. 20, 321-344.
    • (1999) Endocrine Rev. , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 19
    • 0027304028 scopus 로고
    • Estrogens, progestogens, normal breast cell proliferation, and breast cancer risk
    • Pike, M.C., Spicer, D.V., Dahmoush, L., and Press, M.F. (1993). Estrogens, progestogens, normal breast cell proliferation, and breast cancer risk. Epidemiol. Rev. 15, 17-35.
    • (1993) Epidemiol. Rev. , vol.15 , pp. 17-35
    • Pike, M.C.1    Spicer, D.V.2    Dahmoush, L.3    Press, M.F.4
  • 21
    • 0033529557 scopus 로고    scopus 로고
    • Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin ACDK2 complex
    • Rogatsky, I., Trowbridge, J.M., and Garabedian, M.J. (1999). Potentiation of human estrogen receptor α transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin ACDK2 complex. J. Biol. Chem. 274, 22296-22302.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22296-22302
    • Rogatsky, I.1    Trowbridge, J.M.2    Garabedian, M.J.3
  • 22
    • 0345255908 scopus 로고    scopus 로고
    • Nodal signaling in vertebrate development
    • Schier, A.F. (2003). Nodal signaling in vertebrate development. Annu. Rev. Cell Dev. Biol. 19, 589-621.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 589-621
    • Schier, A.F.1
  • 23
    • 0035881568 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-OH Kinase (PI3K)/AKT2, activated in breast cancer, regulates and is induced by estrogen receptor α (ERα) via interaction between ERα and PI3K
    • Sun, M., Paciga, J.E., Feldman, R.I., Yuan, Z., Coppola, D., Lu, Y.Y., Shelley, S.A., Nicosia, S.V., and Cheng, J.Q. (2001). Phosphatidylinositol-3-OH Kinase (PI3K)/AKT2, activated in breast cancer, regulates and is induced by estrogen receptor α (ERα) via interaction between ERα and PI3K. Cancer Res. 61, 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    Shelley, S.A.7    Nicosia, S.V.8    Cheng, J.Q.9
  • 24
    • 0033387743 scopus 로고    scopus 로고
    • FAST-1 is a key maternal effector of mesoderm inducers in the early Xenopus embryo
    • Watanabe, M., and Whitman, M. (1999). FAST-1 is a key maternal effector of mesoderm inducers in the early Xenopus embryo. Development 126, 5621-5634.
    • (1999) Development , vol.126 , pp. 5621-5634
    • Watanabe, M.1    Whitman, M.2
  • 25
    • 0035512155 scopus 로고    scopus 로고
    • Nodal signaling in early vertebrate embryos: Themes and variations
    • Whitman, M. (2001). Nodal signaling in early vertebrate embryos: Themes and variations. Dev. Cell 1, 605-617.
    • (2001) Dev. Cell , vol.1 , pp. 605-617
    • Whitman, M.1
  • 26
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • Xu, J., and Li, Q. (2003). Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 17, 1681-1692.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1681-1692
    • Xu, J.1    Li, Q.2
  • 27
    • 0032110707 scopus 로고    scopus 로고
    • Characterization of human FAST-1, a TGF β and activin signal transducer
    • Zhou, S., Zawel, L., Lengauer, C., Kinzler, K.W., and Vogelstein, B. (1998). Characterization of human FAST-1, a TGF β and activin signal transducer. Mol. Cell 2, 121-127.
    • (1998) Mol. Cell , vol.2 , pp. 121-127
    • Zhou, S.1    Zawel, L.2    Lengauer, C.3    Kinzler, K.W.4    Vogelstein, B.5
  • 28
    • 34547812560 scopus 로고    scopus 로고
    • PKA-induced resistance to tamoxifen is associated with an altered orientation of ERα towards co-activator SRC-1
    • Zwart, W., Griekspoor, A., Berno, V., Lakeman, K., Jalink, K., Mancini, M., Neefjes, J., and Michalides, R. (2007). PKA-induced resistance to tamoxifen is associated with an altered orientation of ERα towards co-activator SRC-1. EMBO J. 26, 3534-3544.
    • (2007) EMBO J. , vol.26 , pp. 3534-3544
    • Zwart, W.1    Griekspoor, A.2    Berno, V.3    Lakeman, K.4    Jalink, K.5    Mancini, M.6    Neefjes, J.7    Michalides, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.