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Volumn 110, Issue 22, 2013, Pages 8894-8899

Interaction of 14-3-3 proteins with the Estrogen Receptor Alpha F domain provides a drug target interface

Author keywords

[No Author keywords available]

Indexed keywords

ESTROGEN RECEPTOR ALPHA; FUSICOCCIN; PROTEIN 14 3 3; THREONINE;

EID: 84878442899     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1220809110     Document Type: Article
Times cited : (113)

References (44)
  • 2
    • 77953384898 scopus 로고    scopus 로고
    • Control of mammary stem cell function by steroid hormone signalling
    • Asselin-Labat M-L, et al. (2010) Control of mammary stem cell function by steroid hormone signalling. Nature 465(7299):798-802.
    • (2010) Nature , vol.465 , Issue.7299 , pp. 798-802
    • Asselin-Labat, M.-L.1
  • 3
    • 84855339741 scopus 로고    scopus 로고
    • Tamoxifen downregulation of miR-451 increases 14-3-3? and promotes breast cancer cell survival and endocrine resistance
    • Bergamaschi A, Katzenellenbogen BS (2012) Tamoxifen downregulation of miR-451 increases 14-3-3? and promotes breast cancer cell survival and endocrine resistance. Oncogene 31(1):39-47.
    • (2012) Oncogene , vol.31 , Issue.1 , pp. 39-47
    • Bergamaschi, A.1    Katzenellenbogen, B.S.2
  • 4
    • 34547812560 scopus 로고    scopus 로고
    • PKA-induced resistance to tamoxifen is associated with an altered orientation of ERalpha towards co-activator SRC-1
    • ZwartW, et al. (2007) PKA-induced resistance to tamoxifen is associated with an altered orientation of ERalpha towards co-activator SRC-1. EMBO J 26(15):3534-3544.
    • (2007) EMBO J , vol.26 , Issue.15 , pp. 3534-3544
    • Zwart, W.1
  • 5
    • 78649335764 scopus 로고    scopus 로고
    • Selectively targeting estrogen receptors for cancer treatment
    • Shanle EK, XuW (2010) Selectively targeting estrogen receptors for cancer treatment. Adv Drug Deliv Rev 62(13):1265-1276.
    • (2010) Adv Drug Deliv Rev , vol.62 , Issue.13 , pp. 1265-1276
    • Shanle, E.K.1    Xu, W.2
  • 6
    • 79958149945 scopus 로고    scopus 로고
    • The turnover of estrogen receptor a by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy
    • Wardell SE, Marks JR, McDonnell DP (2011) The turnover of estrogen receptor a by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy. Biochem Pharmacol 82(2):122-130.
    • (2011) Biochem Pharmacol , vol.82 , Issue.2 , pp. 122-130
    • Wardell, S.E.1    Marks, J.R.2    McDonnell, D.P.3
  • 7
    • 67651123099 scopus 로고    scopus 로고
    • Perturbation of estrogen receptor alpha localization with synthetic nona-arginine LXXLL-peptide coactivator binding inhibitors
    • Carraz M, Zwart W, Phan T, Michalides R, Brunsveld L (2009) Perturbation of estrogen receptor alpha localization with synthetic nona-arginine LXXLL-peptide coactivator binding inhibitors. Chem Biol 16(7):702-711.
    • (2009) Chem Biol , vol.16 , Issue.7 , pp. 702-711
    • Carraz, M.1    Zwart, W.2    Phan, T.3    Michalides, R.4    Brunsveld, L.5
  • 8
    • 77952369277 scopus 로고    scopus 로고
    • Differential requirements of Hsp90 and DNA for the formation of estrogen receptor homodimers and heterodimers
    • Powell E, Wang Y, Shapiro DJ, Xu W (2010) Differential requirements of Hsp90 and DNA for the formation of estrogen receptor homodimers and heterodimers. J Biol Chem 285(21):16125-16134.
    • (2010) J Biol Chem , vol.285 , Issue.21 , pp. 16125-16134
    • Powell, E.1    Wang, Y.2    Shapiro, D.J.3    Xu, W.4
  • 9
    • 84858609310 scopus 로고    scopus 로고
    • Structural basis for Ca2+-induced activation and dimerization of estrogen receptor a by calmodulin
    • Zhang YH, Li ZG, Sacks DB, Ames JB (2012) Structural basis for Ca2+-induced activation and dimerization of estrogen receptor a by calmodulin. J Biol Chem 287(12):9336-9344.
    • (2012) J Biol Chem , vol.287 , Issue.12 , pp. 9336-9344
    • Zhang, Y.H.1    Li, Z.G.2    Sacks, D.B.3    Ames, J.B.4
  • 10
    • 0030667676 scopus 로고    scopus 로고
    • Molecular basis of agonism and antagonism in the oestrogen receptor
    • Brzozowski AM, et al. (1997) Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389(6652):753-758.
    • (1997) Nature , vol.389 , Issue.6652 , pp. 753-758
    • Brzozowski, A.M.1
  • 11
    • 66149125584 scopus 로고    scopus 로고
    • Targeting HSP90 for cancer therapy
    • Mahalingam D, et al. (2009) Targeting HSP90 for cancer therapy. Br J Cancer 100(10): 1523-1529.
    • (2009) Br J Cancer , vol.100 , Issue.10 , pp. 1523-1529
    • Mahalingam, D.1
  • 13
    • 82655181898 scopus 로고    scopus 로고
    • Structural basis for nuclear hormone receptor DNA binding
    • Helsen C, et al. (2012) Structural basis for nuclear hormone receptor DNA binding. Mol Cell Endocrinol 348(2):411-417.
    • (2012) Mol Cell Endocrinol , vol.348 , Issue.2 , pp. 411-417
    • Helsen, C.1
  • 14
    • 57749105457 scopus 로고    scopus 로고
    • Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers
    • Powell E, Xu W (2008) Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers. Proc Natl Acad Sci USA 105(48):19012-19017.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.48 , pp. 19012-19017
    • Powell, E.1    Xu, W.2
  • 15
    • 0032961682 scopus 로고    scopus 로고
    • Estrogen receptor domains E and F: Role in dimerization and interaction with coactivator RIP-140
    • Peters GA, Khan SA (1999) Estrogen receptor domains E and F: Role in dimerization and interaction with coactivator RIP-140. Mol Endocrinol 13(2):286-296.
    • (1999) Mol Endocrinol , vol.13 , Issue.2 , pp. 286-296
    • Peters, G.A.1    Khan, S.A.2
  • 16
    • 40949115376 scopus 로고    scopus 로고
    • The multifunctional estrogen receptor-alpha F domain
    • Skafar DF, Zhao CQ (2008) The multifunctional estrogen receptor-alpha F domain. Endocrine 33(1):1-8.
    • (2008) Endocrine , vol.33 , Issue.1 , pp. 1-8
    • Skafar, D.F.1    Zhao, C.Q.2
  • 17
    • 54849420674 scopus 로고    scopus 로고
    • The F-domain of estrogen receptoralpha inhibits ligand induced receptor dimerization
    • Yang J, SingletonDW, Shaughnessy EA, Khan SA (2008) The F-domain of estrogen receptoralpha inhibits ligand induced receptor dimerization. Mol Cell Endocrinol 295(1-2):94-100.
    • (2008) Mol Cell Endocrinol , vol.295 , Issue.1-2 , pp. 94-100
    • Yang, J.1    Singleton, D.W.2    Shaughnessy, E.A.3    Khan, S.A.4
  • 18
    • 0000765578 scopus 로고
    • Fusicoccin: A New Wilting Toxin produced by Fusicoccum amygdali Del
    • Ballio A, et al. (1964) Fusicoccin: A New Wilting Toxin produced by Fusicoccum amygdali Del. Nature 203(4942):297.
    • (1964) Nature , vol.203 , Issue.4942 , pp. 297
    • Ballio, A.1
  • 19
    • 77952504491 scopus 로고    scopus 로고
    • Fusicoccin-A selectively induces apoptosis in tumor cells after interferon-alpha priming
    • de Vries-van Leeuwen IJ, et al. (2010) Fusicoccin-A selectively induces apoptosis in tumor cells after interferon-alpha priming. Cancer Lett 293(2):198-206.
    • (2010) Cancer Lett , vol.293 , Issue.2 , pp. 198-206
    • De Vries-Van Leeuwen, I.J.1
  • 20
    • 0028535375 scopus 로고
    • A fusicoccin binding protein belongs to the family of 14-3-3 brain protein homologs
    • Korthout HA, de Boer AH (1994) A fusicoccin binding protein belongs to the family of 14-3-3 brain protein homologs. Plant Cell 6(11):1681-1692.
    • (1994) Plant Cell , vol.6 , Issue.11 , pp. 1681-1692
    • Korthout, H.A.1    De Boer, A.H.2
  • 21
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • Würtele M, Jelich-Ottmann C, Wittinghofer A, Oecking C (2003) Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J 22(5):987-994.
    • (2003) EMBO J , vol.22 , Issue.5 , pp. 987-994
    • Würtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 22
    • 33846701051 scopus 로고    scopus 로고
    • Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+-ATPase by combining X-ray crystallography and electron cryomicroscopy
    • Ottmann C, et al. (2007) Structure of a 14-3-3 coordinated hexamer of the plant plasma membrane H+-ATPase by combining X-ray crystallography and electron cryomicroscopy. Mol Cell 25(3):427-440.
    • (2007) Mol Cell , vol.25 , Issue.3 , pp. 427-440
    • Ottmann, C.1
  • 23
    • 58149488988 scopus 로고    scopus 로고
    • The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development
    • Morrison DK (2009) The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development. Trends Cell Biol 19(1):16-23.
    • (2009) Trends Cell Biol , vol.19 , Issue.1 , pp. 16-23
    • Morrison, D.K.1
  • 25
    • 0031252081 scopus 로고    scopus 로고
    • The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase
    • Jahn T, et al. (1997) The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase. Plant Cell 9(10):1805-1814.
    • (1997) Plant Cell , vol.9 , Issue.10 , pp. 1805-1814
    • Jahn, T.1
  • 26
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum DM, Wang Y, Williams SP, Sigler PB (1998) Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA 95(11):5998-6003.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.11 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 27
    • 31944444822 scopus 로고    scopus 로고
    • SWTY-A general peptide probe for homogeneous solution binding assay of 14-3-3 proteins
    • Wu M, et al. (2006) SWTY-a general peptide probe for homogeneous solution binding assay of 14-3-3 proteins. Anal Biochem 349(2):186-196.
    • (2006) Anal Biochem , vol.349 , Issue.2 , pp. 186-196
    • Wu, M.1
  • 28
    • 0001494478 scopus 로고
    • H-1-NMR conformational study of Fusicoccin and related compounds-molecular conformation and biological activity
    • Ballio A, et al. (1991) H-1-NMR conformational study of Fusicoccin and related compounds-molecular conformation and biological activity. Phytochemistry 30(1):137-146.
    • (1991) Phytochemistry , vol.30 , Issue.1 , pp. 137-146
    • Ballio, A.1
  • 29
    • 82455188015 scopus 로고    scopus 로고
    • Oestrogen receptor-co-factor-chromatin specificity in the transcriptional regulation of breast cancer
    • Zwart W, et al. (2011) Oestrogen receptor-co-factor-chromatin specificity in the transcriptional regulation of breast cancer. EMBO J 30(23):4764-4776.
    • (2011) EMBO J , vol.30 , Issue.23 , pp. 4764-4776
    • Zwart, W.1
  • 30
    • 45049086100 scopus 로고    scopus 로고
    • Estrogen and the selective estrogen receptor modulator (SERM) protection against cell death in estrogen receptor alpha and beta expressing U2OS cells
    • Kallio A, et al. (2008) Estrogen and the selective estrogen receptor modulator (SERM) protection against cell death in estrogen receptor alpha and beta expressing U2OS cells. Mol Cell Endocrinol 289(1-2):38-48.
    • (2008) Mol Cell Endocrinol , vol.289 , Issue.1-2 , pp. 38-48
    • Kallio, A.1
  • 31
    • 0142211242 scopus 로고    scopus 로고
    • The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase: Involvement of a region promoting phosphorylationindependent interaction in addition to the phosphorylation-dependent C-terminal end
    • Fuglsang AT, et al. (2003) The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase: Involvement of a region promoting phosphorylationindependent interaction in addition to the phosphorylation- dependent C-terminal end. J Biol Chem 278(43):42266-42272.
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 42266-42272
    • Fuglsang, A.T.1
  • 32
    • 0035955721 scopus 로고    scopus 로고
    • Binding of regulatory 14-3-3 proteins to the C terminus of the plant plasma membrane H+-ATPpase involves part of its autoinhibitory region
    • Jelich-Ottmann C, Weiler EW, Oecking C (2001) Binding of regulatory 14-3-3 proteins to the C terminus of the plant plasma membrane H+-ATPpase involves part of its autoinhibitory region. J Biol Chem 276(43):39852-39857.
    • (2001) J Biol Chem , vol.276 , Issue.43 , pp. 39852-39857
    • Jelich-Ottmann, C.1    Weiler, E.W.2    Oecking, C.3
  • 33
    • 79957949475 scopus 로고    scopus 로고
    • Estrogen receptor-positive breast cancer: A multidisciplinary challenge
    • Zwart W, Theodorou V, Carroll JS (2011) Estrogen receptor-positive breast cancer: A multidisciplinary challenge. Wiley Interdiscip Rev Syst Biol Med 3(2):216-230.
    • (2011) Wiley Interdiscip Rev Syst Biol Med , vol.3 , Issue.2 , pp. 216-230
    • Zwart, W.1    Theodorou, V.2    Carroll, J.S.3
  • 34
    • 79953005347 scopus 로고    scopus 로고
    • Small molecule inhibitors as probes for estrogen and androgen receptor action
    • Shapiro DJ, Mao C, Cherian MT (2011) Small molecule inhibitors as probes for estrogen and androgen receptor action. J Biol Chem 286(6):4043-4048.
    • (2011) J Biol Chem , vol.286 , Issue.6 , pp. 4043-4048
    • Shapiro, D.J.1    Mao, C.2    Cherian, M.T.3
  • 35
    • 80053562371 scopus 로고    scopus 로고
    • Development of subtype-selective oestrogen receptor-based therapeutics
    • Nilsson S, Koehler KF, Gustafsson JA (2011) Development of subtype-selective oestrogen receptor-based therapeutics. Nat Rev Drug Discov 10(10):778-792.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.10 , pp. 778-792
    • Nilsson, S.1    Koehler, K.F.2    Gustafsson, J.A.3
  • 36
    • 77950442251 scopus 로고    scopus 로고
    • Minireview: Not picking pockets: Nuclear receptor alternate-site modulators (NRAMs
    • Moore TW, Mayne CG, Katzenellenbogen JA (2010) Minireview: Not picking pockets: Nuclear receptor alternate-site modulators (NRAMs). Mol Endocrinol 24(4):683-695.
    • (2010) Mol Endocrinol , vol.24 , Issue.4 , pp. 683-695
    • Moore, T.W.1    Mayne, C.G.2    Katzenellenbogen, J.A.3
  • 37
    • 34247889975 scopus 로고    scopus 로고
    • Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions
    • Koide A, et al. (2007) Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Mol Endocrinol 21(4):829-842.
    • (2007) Mol Endocrinol , vol.21 , Issue.4 , pp. 829-842
    • Koide, A.1
  • 38
    • 84875380058 scopus 로고    scopus 로고
    • Plant 14-3-3 proteins as spiders in a web of phosphorylation
    • de Boer AH, van Kleeff PJ, Gao J (2013) Plant 14-3-3 proteins as spiders in a web of phosphorylation. Protoplasma 250(2):425-440.
    • (2013) Protoplasma , vol.250 , Issue.2 , pp. 425-440
    • De Boer, A.H.1    Van Kleeff, P.J.2    Gao, J.3
  • 39
    • 0032188085 scopus 로고    scopus 로고
    • A phosphothreonine residue at the C-terminal end of the plasma membrane H+-ATPase is protected by fusicoccin-induced 14-3-3 binding
    • Olsson A, Svennelid F, Ek B, Sommarin M, Larsson C (1998) A phosphothreonine residue at the C-terminal end of the plasma membrane H+-ATPase is protected by fusicoccin-induced 14-3-3 binding. Plant Physiol 118(2):551-555.
    • (1998) Plant Physiol , vol.118 , Issue.2 , pp. 551-555
    • Olsson, A.1    Svennelid, F.2    Ek, B.3    Sommarin, M.4    Larsson, C.5
  • 40
    • 0035020975 scopus 로고    scopus 로고
    • Analysis of the phosphorylation level in guard-cell plasma membrane H+-ATPase in response to fusicoccin
    • Kinoshita T, Shimazaki K (2001) Analysis of the phosphorylation level in guard-cell plasma membrane H+-ATPase in response to fusicoccin. Plant Cell Physiol 42(4):424-432.
    • (2001) Plant Cell Physiol , vol.42 , Issue.4 , pp. 424-432
    • Kinoshita, T.1    Shimazaki, K.2
  • 41
    • 84868092904 scopus 로고    scopus 로고
    • Estrogen receptor beta binds Sp1 and recruits a corepressor complex to the estrogen receptor alpha gene promoter
    • Bartella V, et al. (2012) Estrogen receptor beta binds Sp1 and recruits a corepressor complex to the estrogen receptor alpha gene promoter. Breast Cancer Res Treat 134(2):569-581.
    • (2012) Breast Cancer Res Treat , vol.134 , Issue.2 , pp. 569-581
    • Bartella, V.1
  • 42
    • 46749108373 scopus 로고    scopus 로고
    • ERbeta in breast cancer-onlooker, passive player, or active protector?
    • Fox EM, Davis RJ, Shupnik MA (2008) ERbeta in breast cancer-onlooker, passive player, or active protector? Steroids 73(11):1039-1051.
    • (2008) Steroids , vol.73 , Issue.11 , pp. 1039-1051
    • Fox, E.M.1    Davis, R.J.2    Shupnik, M.A.3
  • 43
    • 84861886597 scopus 로고    scopus 로고
    • Fusicoccanes: Diterpenes with surprising biological functions
    • de Boer AH, de Vries-van Leeuwen IJ (2012) Fusicoccanes: Diterpenes with surprising biological functions. Trends Plant Sci 17(6):360-368.
    • (2012) Trends Plant Sci , vol.17 , Issue.6 , pp. 360-368
    • De Boer, A.H.1    De Vries-Van Leeuwen, I.J.2
  • 44
    • 33846037859 scopus 로고    scopus 로고
    • 14-3-3 adaptor proteins are intermediates in ABA signal transduction during barley seed germination
    • Schoonheim PJ, et al. (2007) 14-3-3 adaptor proteins are intermediates in ABA signal transduction during barley seed germination. Plant J 49(2):289-301.
    • (2007) Plant J , vol.49 , Issue.2 , pp. 289-301
    • Schoonheim, P.J.1


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