메뉴 건너뛰기




Volumn 21, Issue 10, 2007, Pages 2403-2415

Glucocorticoid-induced degradation of glycogen synthase kinase-3 protein is triggered by serum- and glucocorticoid-induced protein kinase and Akt signaling and controls β-catenin dynamics and tight junction formation in mammary epithelial tumor cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; DEXAMETHASONE; GLUCOCORTICOID; GLYCOGEN SYNTHASE KINASE 3; PROTEIN KINASE; PROTEIN KINASE B;

EID: 34948894886     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2007-0143     Document Type: Article
Times cited : (59)

References (69)
  • 2
    • 0033825953 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity
    • Cereijido M, Shoshani L, Contreras RG 2000 Molecular physiology and pathophysiology of tight junctions. I. Biogenesis of tight junctions and epithelial polarity. Am J Physiol Gastrointest Liver Physiol 279:G477-G482
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Cereijido, M.1    Shoshani, L.2    Contreras, R.G.3
  • 4
    • 0019806209 scopus 로고
    • Membrane asymmetry in epithelia: Is the tight junction a barrier to diffusion in the plasma membrane?
    • Dragsten PR, Blumenthal R, Handler JS 1981 Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane? Nature 294: 718-722
    • (1981) Nature , vol.294 , pp. 718-722
    • Dragsten, P.R.1    Blumenthal, R.2    Handler, J.S.3
  • 6
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara JL 1998 Regulation of the movement of solutes across tight junctions. Annu Rev Physiol 60:143-159
    • (1998) Annu Rev Physiol , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 8
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells
    • van Meer G, Simons K 1986 The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J 5:1455-1464
    • (1986) EMBO J , vol.5 , pp. 1455-1464
    • van Meer, G.1    Simons, K.2
  • 9
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM 1996 Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84:345-357
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 10
    • 0035479827 scopus 로고    scopus 로고
    • Molecular architecture of adherens junctions
    • Nagafuchi A 2001 Molecular architecture of adherens junctions. Curr Opin Cell Biol 13:600-603
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 600-603
    • Nagafuchi, A.1
  • 11
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner B, Stevenson B, Grimaldi A 1988 The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J Cell Biol 107:1575-1587
    • (1988) J Cell Biol , vol.107 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 14
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie CM, Anderson JM 2006 Claudins and epithelial paracellular transport. Annu Rev Physiol 68:403-429
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 15
  • 16
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker BM, Nigam SK 1998 Molecular structure and assembly of the tight junction. Am J Physiol 274:F1-F9
    • (1998) Am J Physiol , vol.274
    • Denker, B.M.1    Nigam, S.K.2
  • 17
    • 0031944250 scopus 로고    scopus 로고
    • Molecular architecture of tight junctions
    • Mitic LL, Anderson JM 1998 Molecular architecture of tight junctions. Annu Rev Physiol 60:121-142
    • (1998) Annu Rev Physiol , vol.60 , pp. 121-142
    • Mitic, L.L.1    Anderson, J.M.2
  • 18
    • 0033672942 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: Nutrients, cytokines, and immune cells
    • Nusrat A, Turner JR, Madara JL 2000 Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: nutrients, cytokines, and immune cells. Am J Physiol Gastrointest Liver Physiol 279:G851-G857
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Nusrat, A.1    Turner, J.R.2    Madara, J.L.3
  • 20
    • 0016260341 scopus 로고
    • Changes in colostrum composition and in the permeability of the mammary epithelium at about the time of parturition in the goat
    • Linzell JL, Peaker M 1974 Changes in colostrum composition and in the permeability of the mammary epithelium at about the time of parturition in the goat. J Physiol 243:129-151
    • (1974) J Physiol , vol.243 , pp. 129-151
    • Linzell, J.L.1    Peaker, M.2
  • 21
    • 0021256942 scopus 로고
    • Electrical potentials and cell-to-cell dye movement in mouse mammary gland during lactation
    • Berga SE 1984 Electrical potentials and cell-to-cell dye movement in mouse mammary gland during lactation. Am J Physiol 247:C20-C25
    • (1984) Am J Physiol , vol.247
    • Berga, S.E.1
  • 23
    • 4344714466 scopus 로고    scopus 로고
    • The organization of tight junctions in epithelia: Implications for mammary gland biology and breast tumorigenesis
    • Itoh M, Bissell MJ 2003 The organization of tight junctions in epithelia: implications for mammary gland biology and breast tumorigenesis. J Mammary Gland Biol Neoplasia 8:449-462
    • (2003) J Mammary Gland Biol Neoplasia , vol.8 , pp. 449-462
    • Itoh, M.1    Bissell, M.J.2
  • 24
    • 0028986713 scopus 로고
    • Transforming growth factor-α abrogates glucocorticoid-stimulated tight junction formation and growth suppression in rat mammary epithelial tumor cells
    • Buse P, Woo PL, Alexander DB, Cha HH, Reza A, Sirota ND, Firestone GL 1995 Transforming growth factor-α abrogates glucocorticoid-stimulated tight junction formation and growth suppression in rat mammary epithelial tumor cells. J Biol Chem 270:6505-6514
    • (1995) J Biol Chem , vol.270 , pp. 6505-6514
    • Buse, P.1    Woo, P.L.2    Alexander, D.B.3    Cha, H.H.4    Reza, A.5    Sirota, N.D.6    Firestone, G.L.7
  • 25
    • 0036346060 scopus 로고    scopus 로고
    • Transforming growth factor-α abrogates the glucocorticoid stimulation of tight junction formation and reverses the steroid-induced down-regulation of fascin in rat mammary epithelial tumor cells by a Ras-dependent pathway
    • Guan Y, Woo PL, Rubenstein EM, Firestone GL 2002 Transforming growth factor-α abrogates the glucocorticoid stimulation of tight junction formation and reverses the steroid-induced down-regulation of fascin in rat mammary epithelial tumor cells by a Ras-dependent pathway. Exp Cell Res 273:1-11
    • (2002) Exp Cell Res , vol.273 , pp. 1-11
    • Guan, Y.1    Woo, P.L.2    Rubenstein, E.M.3    Firestone, G.L.4
  • 26
    • 0033605134 scopus 로고    scopus 로고
    • Glucocorticoid down-regulation of fascin protein expression is required for the steroid-induced formation of tight junctions and cell-cell interactions in rat mammary epithelial tumor cells
    • Wong V, Ching D, McCrea PD, Firestone GL 1999 Glucocorticoid down-regulation of fascin protein expression is required for the steroid-induced formation of tight junctions and cell-cell interactions in rat mammary epithelial tumor cells. J Biol Chem 274:5443-5453
    • (1999) J Biol Chem , vol.274 , pp. 5443-5453
    • Wong, V.1    Ching, D.2    McCrea, P.D.3    Firestone, G.L.4
  • 27
    • 0030067318 scopus 로고    scopus 로고
    • Antagonistic regulation of tight junction dynamics by glucocorticoids and transforming growth factor-β in mouse mammary epithelial cells
    • Woo PL, Cha HH, Singer KL, Firestone GL 1996 Antagonistic regulation of tight junction dynamics by glucocorticoids and transforming growth factor-β in mouse mammary epithelial cells. J Biol Chem 271:404-412
    • (1996) J Biol Chem , vol.271 , pp. 404-412
    • Woo, P.L.1    Cha, H.H.2    Singer, K.L.3    Firestone, G.L.4
  • 28
    • 0032752371 scopus 로고    scopus 로고
    • Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells
    • Woo PL, Ching D, Guan Y, Firestone GL 1999 Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells. J Biol Chem 274:32818-32828
    • (1999) J Biol Chem , vol.274 , pp. 32818-32828
    • Woo, P.L.1    Ching, D.2    Guan, Y.3    Firestone, G.L.4
  • 29
    • 0034666304 scopus 로고    scopus 로고
    • Involvement of the helix-loop-helix protein Id-1 in the glucocorticoid regulation of tight junctions in mammary epithelial cells
    • Woo PL, Cercek A, Desprez PY, Firestone GL 2000 Involvement of the helix-loop-helix protein Id-1 in the glucocorticoid regulation of tight junctions in mammary epithelial cells. J Biol Chem 275:28649-28658
    • (2000) J Biol Chem , vol.275 , pp. 28649-28658
    • Woo, P.L.1    Cercek, A.2    Desprez, P.Y.3    Firestone, G.L.4
  • 30
    • 0038532299 scopus 로고    scopus 로고
    • Glucocorticoid down-regulation of RhoA is required for the steroid-induced organization of the junctional complex and tight junction formation in rat mammary epithelial tumor cells
    • Rubenstein NM, Guan Y, Woo PL, Firestone GL 2003 Glucocorticoid down-regulation of RhoA is required for the steroid-induced organization of the junctional complex and tight junction formation in rat mammary epithelial tumor cells. J Biol Chem 278:10353-10360
    • (2003) J Biol Chem , vol.278 , pp. 10353-10360
    • Rubenstein, N.M.1    Guan, Y.2    Woo, P.L.3    Firestone, G.L.4
  • 32
  • 33
    • 0347916880 scopus 로고    scopus 로고
    • Glucocorticoids control β-catenin protein expression and localization through distinct pathways that can be uncoupled by disruption of signaling events required for tight junction formation in rat mammary epithelial tumor cells
    • Guan Y, Rubenstein HM, Failor KL, Woo PL, Firestone GL 2004 Glucocorticoids control β-catenin protein expression and localization through distinct pathways that can be uncoupled by disruption of signaling events required for tight junction formation in rat mammary epithelial tumor cells. Mol Endocrinol 18:214-227
    • (2004) Mol Endocrinol , vol.18 , pp. 214-227
    • Guan, Y.1    Rubenstein, H.M.2    Failor, K.L.3    Woo, P.L.4    Firestone, G.L.5
  • 34
    • 8444251784 scopus 로고    scopus 로고
    • The Wnt signaling pathway in development and disease
    • Logan CY, Nusse R 2004 The Wnt signaling pathway in development and disease. Annu Rev Cell Dev Biol 20:781-810
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 781-810
    • Logan, C.Y.1    Nusse, R.2
  • 35
    • 0033602227 scopus 로고    scopus 로고
    • Hart M, Concordet JP, Lassot I, Albert I, del los Santos R, Durand H, Perret C, Rubinfeld B, Margottin F, Benarous R, Polakis P 1999 The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell. Curr Biol 9:207-210
    • Hart M, Concordet JP, Lassot I, Albert I, del los Santos R, Durand H, Perret C, Rubinfeld B, Margottin F, Benarous R, Polakis P 1999 The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell. Curr Biol 9:207-210
  • 36
    • 0030806305 scopus 로고    scopus 로고
    • Activation of translation initiation factor eIF2B by insulin requires phosphatidyl inositol 3-kinase
    • Welsh GI, Stokes CM, Wang X, Sakave H, Ogawa W, Kasuga M, Proud CG 1997 Activation of translation initiation factor eIF2B by insulin requires phosphatidyl inositol 3-kinase. FEBS Lett 410:418-422
    • (1997) FEBS Lett , vol.410 , pp. 418-422
    • Welsh, G.I.1    Stokes, C.M.2    Wang, X.3    Sakave, H.4    Ogawa, W.5    Kasuga, M.6    Proud, C.G.7
  • 37
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA 1995 Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378:785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 38
    • 0036073642 scopus 로고    scopus 로고
    • Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 β (GSK-3β) at serine-9 through direct interaction
    • Dai F, Yu L, He H, Chen Y, Yu J, Yang Y, Xu Y, Ling W, Zhao S 2002 Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 β (GSK-3β) at serine-9 through direct interaction. Biochem Biophys Res Commun 293:1191-1196
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 1191-1196
    • Dai, F.1    Yu, L.2    He, H.3    Chen, Y.4    Yu, J.5    Yang, Y.6    Xu, Y.7    Ling, W.8    Zhao, S.9
  • 40
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH 2001 Crystal structure of glycogen synthase kinase 3 β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105:721-732
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 42
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling in development and disease
    • Clevers H 2006 Wnt/β-catenin signaling in development and disease. Cell 127:469-480
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 43
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM 2001 Mechanisms underlying ubiquitination. Annu Rev Biochem 70:503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 44
    • 0027980319 scopus 로고    scopus 로고
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL 1994 Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-771
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL 1994 Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-771
  • 45
    • 0030779038 scopus 로고    scopus 로고
    • Serine phosphorylation-regulated ubiquitination and degradation of β-catenin
    • Orford K, Crockett C, Jensen JP, Weissman AM, Byers SW 1997 Serine phosphorylation-regulated ubiquitination and degradation of β-catenin. J Biol Chem 272:24735-24738
    • (1997) J Biol Chem , vol.272 , pp. 24735-24738
    • Orford, K.1    Crockett, C.2    Jensen, J.P.3    Weissman, A.M.4    Byers, S.W.5
  • 46
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney JD, Hochstrasser M 1999 Substrate targeting in the ubiquitin system. Cell 97:427-430
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 47
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • Jope RS, Johnson GV 2004 The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci 29:95-102
    • (2004) Trends Biochem Sci , vol.29 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.2
  • 48
    • 15844382488 scopus 로고    scopus 로고
    • p53 stimulates promoter activity of the sgk. serum/glucocorticoid-inducible serine/threonine protein kinase gene in rodent mammary epithelial cells
    • Maiyar AC, Huang AJ, Phu PT, Cha HH, Firestone GL 1996 p53 stimulates promoter activity of the sgk. serum/glucocorticoid-inducible serine/threonine protein kinase gene in rodent mammary epithelial cells. J Biol Chem 271:12414-12422
    • (1996) J Biol Chem , vol.271 , pp. 12414-12422
    • Maiyar, A.C.1    Huang, A.J.2    Phu, P.T.3    Cha, H.H.4    Firestone, G.L.5
  • 49
    • 0027534990 scopus 로고
    • Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum
    • Webster MK, Goya L, Ge Y, Maiyar AC, Firestone GL 1993 Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum. Mol Cell Biol 13:2031-2040
    • (1993) Mol Cell Biol , vol.13 , pp. 2031-2040
    • Webster, M.K.1    Goya, L.2    Ge, Y.3    Maiyar, A.C.4    Firestone, G.L.5
  • 50
    • 0033151832 scopus 로고    scopus 로고
    • Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway
    • Park J, Leong ML, Buse P, Maiyar AC, Firestone GL, Hemmings BA 1999 Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. EMBO J 18:3024-3033
    • (1999) EMBO J , vol.18 , pp. 3024-3033
    • Park, J.1    Leong, M.L.2    Buse, P.3    Maiyar, A.C.4    Firestone, G.L.5    Hemmings, B.A.6
  • 51
    • 14444286453 scopus 로고    scopus 로고
    • Insulin stimulation of the fatty acid synthase promoter is mediated by the phosphatidylinositol 3-kinase pathway. Involvement of protein kinase B/Akt
    • Wang D, Sul HS 1998 Insulin stimulation of the fatty acid synthase promoter is mediated by the phosphatidylinositol 3-kinase pathway. Involvement of protein kinase B/Akt. J Biol Chem 273:25420-25426
    • (1998) J Biol Chem , vol.273 , pp. 25420-25426
    • Wang, D.1    Sul, H.S.2
  • 52
    • 0030978351 scopus 로고    scopus 로고
    • β-Catenin is a target for the ubiquitin-proteasome pathway
    • Aberle H, Bauer A, Stappert J, Kispert A, Kemler R 1997 β-Catenin is a target for the ubiquitin-proteasome pathway. EMBO J 16:3797-3804
    • (1997) EMBO J , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 53
    • 1942537708 scopus 로고    scopus 로고
    • The significance of the Wnt pathway in the pathology of human cancers
    • Karim R, Tse G, Putti T, Scolyer R, Lee S 2004 The significance of the Wnt pathway in the pathology of human cancers. Pathology 36:120-128
    • (2004) Pathology , vol.36 , pp. 120-128
    • Karim, R.1    Tse, G.2    Putti, T.3    Scolyer, R.4    Lee, S.5
  • 55
    • 0035135841 scopus 로고    scopus 로고
    • Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)
    • Brunet A, Park J, Tran H, Hu LS, Hemmings BA, Greenberg ME 2001 Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol Cell Biol 21:952-965
    • (2001) Mol Cell Biol , vol.21 , pp. 952-965
    • Brunet, A.1    Park, J.2    Tran, H.3    Hu, L.S.4    Hemmings, B.A.5    Greenberg, M.E.6
  • 57
    • 33748749994 scopus 로고    scopus 로고
    • Lysine residues Lys-19 and Lys-49 of β-catenin regulate its levels and function in T cell factor transcriptional activation and neoplastic transformation
    • Winer IS, Bommer GT, Gonik N, Fearon ER 2006 Lysine residues Lys-19 and Lys-49 of β-catenin regulate its levels and function in T cell factor transcriptional activation and neoplastic transformation. J Biol Chem 281:26181-26187
    • (2006) J Biol Chem , vol.281 , pp. 26181-26187
    • Winer, I.S.1    Bommer, G.T.2    Gonik, N.3    Fearon, E.R.4
  • 59
    • 15444372287 scopus 로고    scopus 로고
    • Essential role of IκB kinase α in the constitutive processing of NF-κB2 p100
    • Qing G, Xiao G 2005 Essential role of IκB kinase α in the constitutive processing of NF-κB2 p100. J Biol Chem 280:9765-9768
    • (2005) J Biol Chem , vol.280 , pp. 9765-9768
    • Qing, G.1    Xiao, G.2
  • 60
    • 0035972159 scopus 로고    scopus 로고
    • Δ N89 β-catenin induces precocious development, differentiation, and neoplasia in mammary gland
    • Imbert A, Eelkema R, Jordan S, Feiner H, Cowin P 2001 Δ N89 β-catenin induces precocious development, differentiation, and neoplasia in mammary gland. J Cell Biol 153:555-568
    • (2001) J Cell Biol , vol.153 , pp. 555-568
    • Imbert, A.1    Eelkema, R.2    Jordan, S.3    Feiner, H.4    Cowin, P.5
  • 61
    • 13244265798 scopus 로고    scopus 로고
    • Changes in the Wnt signalling pathway in gastrointestinal cancers and their prognostic significance
    • Doucas H, Garcea G, Neal CP, Manson MM, Berry DP 2005 Changes in the Wnt signalling pathway in gastrointestinal cancers and their prognostic significance. Eur J Cancer 41:365-379
    • (2005) Eur J Cancer , vol.41 , pp. 365-379
    • Doucas, H.1    Garcea, G.2    Neal, C.P.3    Manson, M.M.4    Berry, D.P.5
  • 62
    • 33846193290 scopus 로고    scopus 로고
    • The many ways of Wnt in cancer
    • Polakis P 2007 The many ways of Wnt in cancer. Curr Opin Genet Dev 17:45-51
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 45-51
    • Polakis, P.1
  • 63
    • 13944259795 scopus 로고    scopus 로고
    • Targeted activation of β-catenin signaling in basal mammary epithelial cells affects mammary development and leads to hyperplasia
    • Teuliere J, Faraldo MM, Deugnier MA, Shtutman M, Ben-Ze'ev A, Thiery JP, Glukhova MA 2005 Targeted activation of β-catenin signaling in basal mammary epithelial cells affects mammary development and leads to hyperplasia. Development 132:267-277
    • (2005) Development , vol.132 , pp. 267-277
    • Teuliere, J.1    Faraldo, M.M.2    Deugnier, M.A.3    Shtutman, M.4    Ben-Ze'ev, A.5    Thiery, J.P.6    Glukhova, M.A.7
  • 64
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble BW, Woodgett JR 2003 GSK-3: tricks of the trade for a multi-tasking kinase. J Cell Sci 116:1175-1186
    • (2003) J Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 65
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β phosphorylates τ at both primed and unprimed sites. Differential impact on microtubule binding
    • Cho JH, Johnson GV 2003 Glycogen synthase kinase 3β phosphorylates τ at both primed and unprimed sites. Differential impact on microtubule binding. J Biol Chem 278:187-193
    • (2003) J Biol Chem , vol.278 , pp. 187-193
    • Cho, J.H.1    Johnson, G.V.2
  • 66
    • 0036090823 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: An emerging therapeutic target
    • Eldar-Finkelman H 2002 Glycogen synthase kinase 3: an emerging therapeutic target. Trends Mol Med 8:126-132
    • (2002) Trends Mol Med , vol.8 , pp. 126-132
    • Eldar-Finkelman, H.1
  • 67
    • 0032947795 scopus 로고    scopus 로고
    • Anti-bipolar therapy: Mechanism of action of lithium
    • Jope RS 1999 Anti-bipolar therapy: mechanism of action of lithium. Mol Psychiatry 4:117-128
    • (1999) Mol Psychiatry , vol.4 , pp. 117-128
    • Jope, R.S.1
  • 68
  • 69
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • Phiel CJ, Wilson CA, Lee VM, Klein PS 2003 GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature 423:435-439
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.