메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Lysosomal function is involved in 17β-estradiol-induced estrogen receptor α degradation and cell proliferation

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROQUINE; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; PROTEASOME; TRANSIENT RECEPTOR POTENTIAL CHANNEL M2;

EID: 84899671764     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094880     Document Type: Article
Times cited : (42)

References (36)
  • 1
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks - A driver for protein function in evolution
    • Powers ET, Balch WE (2013) Diversity in the origins of proteostasis networks-a driver for protein function in evolution. Nat Rev Mol Cell Biol 14: 237-248.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 2
    • 75749096347 scopus 로고    scopus 로고
    • The endocytic matrix
    • Scita G, Di Fiore PP (2010) The endocytic matrix. Nature 463: 464-473.
    • (2010) Nature , vol.463 , pp. 464-473
    • Scita, G.1    Di Fiore, P.P.2
  • 3
    • 84899980881 scopus 로고    scopus 로고
    • Proteasomal and lysosomal protein degradation and heart disease
    • Wang X, Robbins J (2013) Proteasomal and lysosomal protein degradation and heart disease. J Mol Cell Cardiol.
    • (2013) J Mol Cell Cardiol
    • Wang, X.1    Robbins, J.2
  • 4
    • 84860319025 scopus 로고    scopus 로고
    • The effects of 17b-estradiol in cancer are mediated by estrogen receptor signaling at the plasma membrane
    • Acconcia F, Marino M (2011) The effects of 17b-estradiol in cancer are mediated by estrogen receptor signaling at the plasma membrane. Frontiers in PHYSIOLOGY 2: 30.
    • (2011) Frontiers in PHYSIOLOGY , vol.2 , pp. 30
    • Acconcia, F.1    Marino, M.2
  • 5
    • 11144332004 scopus 로고    scopus 로고
    • Palmitoylation-dependent estrogen receptor alpha membrane localization: Regulation by 17 beta-estradiol
    • Acconcia F, Ascenzi P, Bocedi A, Spisni E, Tomasi V, et al. (2005) Palmitoylation-dependent estrogen receptor alpha membrane localization: Regulation by 17 beta-estradiol. Molecular Biology of the Cell 16: 231-237.
    • (2005) Molecular Biology of the Cell , vol.16 , pp. 231-237
    • Acconcia, F.1    Ascenzi, P.2    Bocedi, A.3    Spisni, E.4    Tomasi, V.5
  • 6
    • 84860320810 scopus 로고    scopus 로고
    • Palmitoylation Regulates 17beta-Estradiol-Induced Estrogen Receptor-alpha Degradation and Transcriptional Activity
    • La Rosa P, Pesiri V, Leclercq G, Marino M, Acconcia F (2012) Palmitoylation Regulates 17beta-Estradiol-Induced Estrogen Receptor-alpha Degradation and Transcriptional Activity. Mol Endocrinol 26: 762-774.
    • (2012) Mol Endocrinol , vol.26 , pp. 762-774
    • La Rosa, P.1    Pesiri, V.2    Leclercq, G.3    Marino, M.4    Acconcia, F.5
  • 7
    • 84855398593 scopus 로고    scopus 로고
    • DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors
    • Pedram A, Razandi M, Deschenes RJ, Levin ER (2012) DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors. Mol Biol Cell 23: 188-199.
    • (2012) Mol Biol Cell , vol.23 , pp. 188-199
    • Pedram, A.1    Razandi, M.2    Deschenes, R.J.3    Levin, E.R.4
  • 8
    • 34547928773 scopus 로고    scopus 로고
    • A conserved mechanism for steroid receptor translocation to the plasma membrane
    • Pedram A, Razandi M, Sainson RC, Kim JK, Hughes CC, et al. (2007) A conserved mechanism for steroid receptor translocation to the plasma membrane. J Biol Chem 282: 22278-22288.
    • (2007) J Biol Chem , vol.282 , pp. 22278-22288
    • Pedram, A.1    Razandi, M.2    Sainson, R.C.3    Kim, J.K.4    Hughes, C.C.5
  • 9
    • 84892595887 scopus 로고    scopus 로고
    • Mutation of the palmitoylation site of estrogen receptor alpha in vivo reveals tissue-specific roles for membrane versus nuclear actions
    • Adlanmerini M, Solinhac R, Abot A, Fabre A, Raymond-Letron I, et al. (2014) Mutation of the palmitoylation site of estrogen receptor alpha in vivo reveals tissue-specific roles for membrane versus nuclear actions. Proc Natl Acad Sci U S A 111: E283-290.
    • (2014) Proc Natl Acad Sci U S A , vol.111
    • Adlanmerini, M.1    Solinhac, R.2    Abot, A.3    Fabre, A.4    Raymond-Letron, I.5
  • 10
    • 81255160756 scopus 로고    scopus 로고
    • Signaling functions of ubiquitin in the 17betaestradiol (E2):estrogen receptor (ER) alpha network
    • La Rosa P, Acconcia F (2011) Signaling functions of ubiquitin in the 17betaestradiol (E2):estrogen receptor (ER) alpha network. J Steroid Biochem Mol Biol 127: 223-230.
    • (2011) J Steroid Biochem Mol Biol , vol.127 , pp. 223-230
    • La Rosa, P.1    Acconcia, F.2
  • 11
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R, Penot G, Hubner MR, Reid G, Brand H, et al. (2003) Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115: 751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5
  • 12
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • Reid G, Hubner MR, Metivier R, Brand H, Denger S, et al. (2003) Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha 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
  • 14
    • 0021216779 scopus 로고
    • Specific internalization of estrogen and binding to nuclear matrix in isolated uterine cells
    • Pietras RJ, Szego CM (1984) Specific internalization of estrogen and binding to nuclear matrix in isolated uterine cells. Biochem Biophys Res Commun 123: 84-91.
    • (1984) Biochem Biophys Res Commun , vol.123 , pp. 84-91
    • Pietras, R.J.1    Szego, C.M.2
  • 15
    • 0033830222 scopus 로고    scopus 로고
    • Electron microscopic visualization of membrane-mediated uptake and translocation of estrogen-BSA:colloidal gold by hep G2 cells
    • Moats RK, 2nd, Ramirez VD (2000) Electron microscopic visualization of membrane-mediated uptake and translocation of estrogen-BSA:colloidal gold by hep G2 cells. J Endocrinol 166: 631-647.
    • (2000) J Endocrinol , vol.166 , pp. 631-647
    • Moats, I.I.R.K.1    Ramirez, V.D.2
  • 16
    • 84899701444 scopus 로고    scopus 로고
    • Fluorescently-Labeled Estradiol Internalization and Membrane Trafficking in Live N-38 Neuronal Cells Visualized with Total Internal Reflection Fluorescence Microscopy
    • Kisler K, Chow RH, Dominguez R (2013) Fluorescently-Labeled Estradiol Internalization and Membrane Trafficking in Live N-38 Neuronal Cells Visualized with Total Internal Reflection Fluorescence Microscopy. J Steroids Horm Sci Suppl 12.
    • (2013) J Steroids Horm Sci Suppl , pp. 12
    • Kisler, K.1    Chow, R.H.2    Dominguez, R.3
  • 17
    • 18044362733 scopus 로고    scopus 로고
    • Role of the proteasome in the regulation of estrogen receptor alpha turnover and function in MCF-7 breast carcinoma cells
    • Laios I, Journe F, Nonclercq D, Vidal DS, Toillon RA, et al. (2005) Role of the proteasome in the regulation of estrogen receptor alpha turnover and function in MCF-7 breast carcinoma cells. J Steroid Biochem Mol Biol 94: 347-359.
    • (2005) J Steroid Biochem Mol Biol , vol.94 , pp. 347-359
    • Laios, I.1    Journe, F.2    Nonclercq, D.3    Vidal, D.S.4    Toillon, R.A.5
  • 18
    • 84856698420 scopus 로고    scopus 로고
    • Endocytosis and signaling: Cell logistics shape the eukaryotic cell plan
    • Sigismund S, Confalonieri S, Ciliberto A, Polo S, Scita G, et al. (2012) Endocytosis and signaling: cell logistics shape the eukaryotic cell plan. Physiol Rev 92: 273-366.
    • (2012) Physiol Rev , vol.92 , pp. 273-366
    • Sigismund, S.1    Confalonieri, S.2    Ciliberto, A.3    Polo, S.4    Scita, G.5
  • 20
    • 0037377558 scopus 로고    scopus 로고
    • Epitope-dependent localization of estrogen receptor-alpha, but not -beta, in en face arterial endothelium
    • Dan P, Cheung JC, Scriven DR, Moore ED (2003) Epitope-dependent localization of estrogen receptor-alpha, but not -beta, in en face arterial endothelium. Am J Physiol Heart Circ Physiol 284: H1295-1306.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Dan, P.1    Cheung, J.C.2    Scriven, D.R.3    Moore, E.D.4
  • 21
    • 79953300720 scopus 로고    scopus 로고
    • Selective mutations in estrogen receptor alpha D-domain alters nuclear translocation and nonestrogen response element gene regulatory mechanisms
    • Burns KA, Li Y, Arao Y, Petrovich RM, Korach KS (2011) Selective mutations in estrogen receptor alpha D-domain alters nuclear translocation and nonestrogen response element gene regulatory mechanisms. J Biol Chem 286: 12640-12649.
    • (2011) J Biol Chem , vol.286 , pp. 12640-12649
    • Burns, K.A.1    Li, Y.2    Arao, Y.3    Petrovich, R.M.4    Korach, K.S.5
  • 24
    • 14744283561 scopus 로고    scopus 로고
    • Survival versus apoptotic 17beta-estradiol effect: Role of ER alpha and ER beta activated nongenomic signaling
    • Acconcia F, Totta P, Ogawa S, Cardillo I, Inoue S, et al. (2005) Survival versus apoptotic 17beta-estradiol effect: role of ER alpha and ER beta activated nongenomic signaling. J Cell Physiol 203: 193-201.
    • (2005) J Cell Physiol , vol.203 , pp. 193-201
    • Acconcia, F.1    Totta, P.2    Ogawa, S.3    Cardillo, I.4    Inoue, S.5
  • 25
    • 17944375553 scopus 로고    scopus 로고
    • PI3-kinase in concert with Src promotes the S-phase entry of oestradiolstimulated MCF-7 cells
    • Castoria G, Migliaccio A, Bilancio A, Di Domenico M, de Falco A, et al. (2001) PI3-kinase in concert with Src promotes the S-phase entry of oestradiolstimulated MCF-7 cells. EMBO J 20: 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
  • 26
    • 33644871076 scopus 로고    scopus 로고
    • Estrogen receptor alpha: Impact of ligands on intracellular shuttling and turnover rate in breast cancer cells
    • Leclercq G, Lacroix M, Laios I, Laurent G (2006) Estrogen receptor alpha: impact of ligands on intracellular shuttling and turnover rate in breast cancer cells. Curr Cancer Drug Targets 6: 39-64.
    • (2006) Curr Cancer Drug Targets , vol.6 , pp. 39-64
    • Leclercq, G.1    Lacroix, M.2    Laios, I.3    Laurent, G.4
  • 27
    • 46349108800 scopus 로고    scopus 로고
    • Estrogen receptor-alpha hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome
    • Berry NB, Fan M, Nephew KP (2008) Estrogen receptor-alpha hinge-region lysines 302 and 303 regulate receptor degradation by the proteasome. Mol Endocrinol 22: 1535-1551.
    • (2008) Mol Endocrinol , vol.22 , pp. 1535-1551
    • Berry, N.B.1    Fan, M.2    Nephew, K.P.3
  • 28
    • 48549088895 scopus 로고    scopus 로고
    • Clathrinmediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund S, Argenzio E, Tosoni D, Cavallaro E, Polo S, et al. (2008) Clathrinmediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Developmental Cell 15: 209-219.
    • (2008) Developmental Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5
  • 29
    • 79960081347 scopus 로고    scopus 로고
    • Identification of a lysosomal pathway that modulates glucocorticoid signaling and the inflammatory response
    • He Y, Xu Y, Zhang C, Gao X, Dykema KJ, et al. (2013) Identification of a lysosomal pathway that modulates glucocorticoid signaling and the inflammatory response. Sci Signal 4: ra44.
    • (2013) Sci Signal , vol.4
    • He, Y.1    Xu, Y.2    Zhang, C.3    Gao, X.4    Dykema, K.J.5
  • 30
    • 8344241132 scopus 로고    scopus 로고
    • Inhibiting proteasomal proteolysis sustains estrogen receptor-alpha activation
    • Fan M, Nakshatri H, Nephew KP (2004) Inhibiting proteasomal proteolysis sustains estrogen receptor-alpha activation. Mol Endocrinol 18: 2603-2615.
    • (2004) Mol Endocrinol , vol.18 , pp. 2603-2615
    • Fan, M.1    Nakshatri, H.2    Nephew, K.P.3
  • 31
    • 71749096160 scopus 로고    scopus 로고
    • Chloroquine and its analogs: A new promise of an old drug for effective and safe cancer therapies
    • Solomon VR, Lee H (2009) Chloroquine and its analogs: a new promise of an old drug for effective and safe cancer therapies. Eur J Pharmacol 625: 220-233.
    • (2009) Eur J Pharmacol , vol.625 , pp. 220-233
    • Solomon, V.R.1    Lee, H.2
  • 32
    • 84876936620 scopus 로고    scopus 로고
    • Repurposing the antimycotic drug flucytosine for suppression of Pseudomonas aeruginosa pathogenicity
    • Imperi F, Massai F, Facchini M, Frangipani E, Visaggio D, et al. (2013) Repurposing the antimycotic drug flucytosine for suppression of Pseudomonas aeruginosa pathogenicity. Proc Natl Acad Sci U S A 110: 7458-7463.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7458-7463
    • Imperi, F.1    Massai, F.2    Facchini, M.3    Frangipani, E.4    Visaggio, D.5
  • 33
    • 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, Levin ER (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
  • 35
    • 33744943264 scopus 로고    scopus 로고
    • Signaling regulation of genomic and nongenomic functions of estrogen receptors
    • Acconcia F, Kumar R (2006) Signaling regulation of genomic and nongenomic functions of estrogen receptors. Cancer Letters 238: 1-14.
    • (2006) Cancer Letters , vol.238 , pp. 1-14
    • Acconcia, F.1    Kumar, R.2
  • 36
    • 79954421269 scopus 로고    scopus 로고
    • 17 beta-Estradiol-induced cell proliferation requires estrogen receptor (ER) alpha monoubiquitination
    • La Rosa P, Pesiri V, Marino M, Acconcia F (2011) 17 beta-Estradiol- induced cell proliferation requires estrogen receptor (ER) alpha monoubiquitination. Cellular Signalling 23: 1128-1135.
    • (2011) Cellular Signalling , vol.23 , pp. 1128-1135
    • La Rosa, P.1    Pesiri, V.2    Marino, M.3    Acconcia, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.