메뉴 건너뛰기




Volumn 30, Issue 3, 2010, Pages 745-763

Pin1 facilitates the phosphorylation-dependent ubiquitination of SF-1 to regulate gonadotropin β-subunit gene transcription

Author keywords

[No Author keywords available]

Indexed keywords

GONADORELIN; GONADOTROPIN; GONADOTROPIN BETA; PEPTIDYLPROLYL ISOMERASE PIN1; SERINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR EGR 1; TRANSCRIPTION FACTOR PITX1; TRANSCRIPTION FACTOR SF1; UNCLASSIFIED DRUG;

EID: 75149185157     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00807-09     Document Type: Article
Times cited : (29)

References (71)
  • 1
    • 0345169165 scopus 로고    scopus 로고
    • Spermatogonial depletion in adult Pin1-deficient mice
    • Atchison, F. W., and A. R. Means. 2003. Spermatogonial depletion in adult Pin1-deficient mice. Biol. Reprod. 69:1989-1997.
    • (2003) Biol. Reprod , vol.69 , pp. 1989-1997
    • Atchison, F.W.1    Means, A.R.2
  • 2
    • 0036726532 scopus 로고    scopus 로고
    • Signal-induced site specific phosphorylation targets Bcl2 to the proteasome pathway
    • Basu, A., and S. Haldar. 2002. Signal-induced site specific phosphorylation targets Bcl2 to the proteasome pathway. Int. J. Oncol. 21:597-601.
    • (2002) Int. J. Oncol , vol.21 , pp. 597-601
    • Basu, A.1    Haldar, S.2
  • 3
    • 65149105339 scopus 로고    scopus 로고
    • A post-translational modification code for transcription factors: Sorting through a sea of signals
    • Benayoun, B. A., and R. A. Veitia. 2009. A post-translational modification code for transcription factors: sorting through a sea of signals. Trends Cell Biol. 19:189-197.
    • (2009) Trends Cell Biol , vol.19 , pp. 189-197
    • Benayoun, B.A.1    Veitia, R.A.2
  • 4
    • 0035900792 scopus 로고    scopus 로고
    • Ras induces elevation of E2F-1 mRNA levels
    • Berkovich, E., and D. Ginsberg. 2001. Ras induces elevation of E2F-1 mRNA levels. J. Biol. Chem. 276:42851-42856.
    • (2001) J. Biol. Chem , vol.276 , pp. 42851-42856
    • Berkovich, E.1    Ginsberg, D.2
  • 6
    • 35148878581 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors reduce steroidogenesis through SCF-mediated ubiquitination and degradation of steroidogenic factor 1 (NR5A1)
    • Chen, W. Y., J. H. Weng, C. C. Huang, and B. C. Chung. 2007. Histone deacetylase inhibitors reduce steroidogenesis through SCF-mediated ubiquitination and degradation of steroidogenic factor 1 (NR5A1). Mol. Cell. Biol. 27:7284-7290.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 7284-7290
    • Chen, W.Y.1    Weng, J.H.2    Huang, C.C.3    Chung, B.C.4
  • 7
    • 0347683480 scopus 로고    scopus 로고
    • A novel AP-1 site is critical for maximal induction of the follicle-stimulating hormone β gene by gonadotropin-releasing hormone
    • Coss, D., S. B. Jacobs, C. E. Bender, and P. L. Mellon. 2004. A novel AP-1 site is critical for maximal induction of the follicle-stimulating hormone β gene by gonadotropin-releasing hormone. J. Biol. Chem. 279:152-162.
    • (2004) J. Biol. Chem , vol.279 , pp. 152-162
    • Coss, D.1    Jacobs, S.B.2    Bender, C.E.3    Mellon, P.L.4
  • 9
    • 0036787839 scopus 로고    scopus 로고
    • Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1
    • Desclozeaux, M., I. N. Krylova, F. Horn, R. J. Fletterick, and H. A. Ingraham. 2002. Phosphorylation and intramolecular stabilization of the ligand binding domain in the nuclear receptor steroidogenic factor 1. Mol. Cell. Biol. 22:7193-7203.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7193-7203
    • Desclozeaux, M.1    Krylova, I.N.2    Horn, F.3    Fletterick, R.J.4    Ingraham, H.A.5
  • 10
    • 0033553473 scopus 로고    scopus 로고
    • Activation of Luteinizing hormone gene by gonadotropin-releasing hormone requires the synergy of early growth response-1 and steroidogenic factor-1
    • Dorn, C., Q. Ou, J. Svaren, P. A. Crawford, and Y. Sadovsky. 1999. Activation of Luteinizing hormone gene by gonadotropin-releasing hormone requires the synergy of early growth response-1 and steroidogenic factor-1. J. Biol. Chem. 274:13870-13876.
    • (1999) J. Biol. Chem , vol.274 , pp. 13870-13876
    • Dorn, C.1    Ou, Q.2    Svaren, J.3    Crawford, P.A.4    Sadovsky, Y.5
  • 11
    • 50849133904 scopus 로고    scopus 로고
    • A proteomic comparison of immature and mature mouse gonadotrophs reveals novel differentially expressed nuclear proteins that regulate gonadotropin gene transcription and RNA splicing
    • Feng, J., M. A. Lawson, and P. Melamed. 2008. A proteomic comparison of immature and mature mouse gonadotrophs reveals novel differentially expressed nuclear proteins that regulate gonadotropin gene transcription and RNA splicing. Biol. Reprod. 79:546-561.
    • (2008) Biol. Reprod , vol.79 , pp. 546-561
    • Feng, J.1    Lawson, M.A.2    Melamed, P.3
  • 12
    • 0242330293 scopus 로고    scopus 로고
    • Steroidogenic factor-1 and the gonadotrope-specific element enhance basal and pituitary adenylate cyclase-activating polypeptide-stimulated transcription of the human glycoprotein hormone α-subunit gene in gonadotropes
    • Fowkes, R. C., M. Desclozeaux, M. V. Patel, S. J. B. Aylwin, P. King, H. A. Ingraham, and J. M. Burrin. 2003. Steroidogenic factor-1 and the gonadotrope-specific element enhance basal and pituitary adenylate cyclase-activating polypeptide-stimulated transcription of the human glycoprotein hormone α-subunit gene in gonadotropes. Mol. Endocrinol. 17:2177-2188.
    • (2003) Mol. Endocrinol , vol.17 , pp. 2177-2188
    • Fowkes, R.C.1    Desclozeaux, M.2    Patel, M.V.3    Aylwin, S.J.B.4    King, P.5    Ingraham, H.A.6    Burrin, J.M.7
  • 13
    • 0034747803 scopus 로고    scopus 로고
    • Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop
    • Garrett, S., W. A. Barton, R. Knights, P. Jin, D. O. Morgan, and R. P. Fisher. 2001. Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop. Mol. Cell. Biol. 21:88-99.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 88-99
    • Garrett, S.1    Barton, W.A.2    Knights, R.3    Jin, P.4    Morgan, D.O.5    Fisher, R.P.6
  • 15
    • 0032893316 scopus 로고    scopus 로고
    • The protein kinase C system acts through the early growth response protein 1 to increase LHβ gene expression in synergy with steroidogenic factor-1
    • Halvorson, L. M., U. B. Kaiser, and W. W. Chin. 1999. The protein kinase C system acts through the early growth response protein 1 to increase LHβ gene expression in synergy with steroidogenic factor-1. Mol. Endocrinol. 13:106-116.
    • (1999) Mol. Endocrinol , vol.13 , pp. 106-116
    • Halvorson, L.M.1    Kaiser, U.B.2    Chin, W.W.3
  • 16
    • 0033120086 scopus 로고    scopus 로고
    • Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: Integration of hormone signaling in reproduction and stress
    • Hammer, G. D., I. Krylova, Y. Zhang, B. D. Darimont, K. Simpson, N. L. Weigel, and H. A. Ingraham. 1999. Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: Integration of hormone signaling in reproduction and stress. Mol. Cell 3:521-526.
    • (1999) Mol. Cell , vol.3 , pp. 521-526
    • Hammer, G.D.1    Krylova, I.2    Zhang, Y.3    Darimont, B.D.4    Simpson, K.5    Weigel, N.L.6    Ingraham, H.A.7
  • 17
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. 2001. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:195-201.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 19
    • 4143096239 scopus 로고    scopus 로고
    • Multiple and overlapping combinatorial codes orchestrate hormonal responsiveness and dictate cell-specific expression of the genes encoding luteinizing hormone
    • Jorgensen, J. S., C. C. Quirk, and J. H. Nilson. 2004. Multiple and overlapping combinatorial codes orchestrate hormonal responsiveness and dictate cell-specific expression of the genes encoding luteinizing hormone. Endocr. Rev. 25:521-542.
    • (2004) Endocr. Rev , vol.25 , pp. 521-542
    • Jorgensen, J.S.1    Quirk, C.C.2    Nilson, J.H.3
  • 20
    • 0032557554 scopus 로고    scopus 로고
    • Sp1 binds to the rat luteinizing hormone β (LHβ) gene promoter and mediates gonadotropin-releasing hormone-stimulated expression of the LHβ subunit gene
    • Kaiser, U. B., E. Sabbagh, M. T. Chen, W. W. Chin, and B. D. Saunders. 1998. Sp1 binds to the rat luteinizing hormone β (LHβ) gene promoter and mediates gonadotropin-releasing hormone-stimulated expression of the LHβ subunit gene. J. Biol. Chem. 273:12943-12951.
    • (1998) J. Biol. Chem , vol.273 , pp. 12943-12951
    • Kaiser, U.B.1    Sabbagh, E.2    Chen, M.T.3    Chin, W.W.4    Saunders, B.D.5
  • 21
    • 0034465050 scopus 로고    scopus 로고
    • Sp1, steroidogenic factor 1 (SF-1), and early growth response protein 1 (egr-1) binding sites form a tripartite gonadotropin-releasing hormone response element in the rat luteinizing hormone-β gene promoter: An integral role for SF-1
    • Kaiser, U. B., L. M. Halvorson, and M. T. Chen. 2000. Sp1, steroidogenic factor 1 (SF-1), and early growth response protein 1 (egr-1) binding sites form a tripartite gonadotropin-releasing hormone response element in the rat luteinizing hormone-β gene promoter: an integral role for SF-1. Mol. Endocrinol. 14:1235-1245.
    • (2000) Mol. Endocrinol , vol.14 , pp. 1235-1245
    • Kaiser, U.B.1    Halvorson, L.M.2    Chen, M.T.3
  • 22
    • 5044236130 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9
    • Komatsu, T., H. Mizusaki, T. Mukai, H. Ogawa, D. Baba, M. Shirakawa, S. Hatakeyama, K. I. Nakayama, H. Yamamoto, A. Kikuchi, and K. Morohashi. 2004. Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9. Mol. Endocrinol. 18:2451-2462.
    • (2004) Mol. Endocrinol , vol.18 , pp. 2451-2462
    • Komatsu, T.1    Mizusaki, H.2    Mukai, T.3    Ogawa, H.4    Baba, D.5    Shirakawa, M.6    Hatakeyama, S.7    Nakayama, K.I.8    Yamamoto, H.9    Kikuchi, A.10    Morohashi, K.11
  • 23
    • 42549138372 scopus 로고    scopus 로고
    • Paired-like homeodomain transcription factors 1 and 2 regulate follicle-stimulating hormone β-subunit transcription through a conserved ciselement
    • Lamba, P., V. Khivansara, A. C. D'Alessio, M. M. Santos, and D. J. Bernard. 2008. Paired-like homeodomain transcription factors 1 and 2 regulate follicle-stimulating hormone β-subunit transcription through a conserved ciselement. Endocrinology 149:3095-3108.
    • (2008) Endocrinology , vol.149 , pp. 3095-3108
    • Lamba, P.1    Khivansara, V.2    D'Alessio, A.C.3    Santos, M.M.4    Bernard, D.J.5
  • 24
  • 25
    • 0030822865 scopus 로고    scopus 로고
    • The bicoid-related homeoprotein Ptx1 defines the most anterior domain of the embryo and differentiates posterior from anterior lateral mesoderm
    • Lanctôt, C., B. Lamolet, and J. Drouin. 1997. The bicoid-related homeoprotein Ptx1 defines the most anterior domain of the embryo and differentiates posterior from anterior lateral mesoderm. Development 124:2807-2817.
    • (1997) Development , vol.124 , pp. 2807-2817
    • Lanctôt, C.1    Lamolet, B.2    Drouin, J.3
  • 26
    • 13544259457 scopus 로고    scopus 로고
    • The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification
    • Lee, M. B., L. A. Lebedeva, M. Suzawa, S. A. Wadekar, M. Desclozeaux, and H. A. Ingraham. 2005. The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification. Mol. Cell. Biol. 25:1879-1890.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1879-1890
    • Lee, M.B.1    Lebedeva, L.A.2    Suzawa, M.3    Wadekar, S.A.4    Desclozeaux, M.5    Ingraham, H.A.6
  • 29
    • 70349655659 scopus 로고    scopus 로고
    • Negative feedback governs gonadotrope frequency-decoding of gonadotropin releasing hormone pulse-frequency
    • Lim, S., L. Pnueli, J. H. Tan, Z. Naor, G. Rajagopal, and P. Melamed. 2009. Negative feedback governs gonadotrope frequency-decoding of gonadotropin releasing hormone pulse-frequency. PLoS One 29:e7244.
    • (2009) PLoS One , vol.29
    • Lim, S.1    Pnueli, L.2    Tan, J.H.3    Naor, Z.4    Rajagopal, G.5    Melamed, P.6
  • 30
    • 34347361646 scopus 로고    scopus 로고
    • Lim, S., M. Luo, M. Koh, M. Yang, M. N. bin Abdul Kadir, J. H. Tan, Z. Ye, W. Wang, and P. Melamed. 2007. Distinct mechanisms involving diverse histone deacetylases repress expression of the two gonadotropin -subunit genes in immature gonadotropes, and their actions are overcome by gonadotropin- releasing hormone. Mol. Cell. Biol. 27:4105-4120.
    • Lim, S., M. Luo, M. Koh, M. Yang, M. N. bin Abdul Kadir, J. H. Tan, Z. Ye, W. Wang, and P. Melamed. 2007. Distinct mechanisms involving diverse histone deacetylases repress expression of the two gonadotropin -subunit genes in immature gonadotropes, and their actions are overcome by gonadotropin- releasing hormone. Mol. Cell. Biol. 27:4105-4120.
  • 33
    • 34548660854 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer
    • Lu, K. P., G. Finn, T. H. Lee, and L. K. Nicholson. 2007. Prolyl cis-trans isomerization as a molecular timer. Nat. Chem. Biol. 3:619-629.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 619-629
    • Lu, K.P.1    Finn, G.2    Lee, T.H.3    Nicholson, L.K.4
  • 34
    • 35448945269 scopus 로고    scopus 로고
    • The prolyl isomerase PIN1: A pivotal new twist in phosphorylation signalling and disease
    • Lu, K. P., and X. Z. Zhou. 2007. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease. Nat. Rev. Mol. Cell Biol. 8:904-916.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 904-916
    • Lu, K.P.1    Zhou, X.Z.2
  • 35
    • 0037169479 scopus 로고    scopus 로고
    • Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function
    • Lu, P. J., X. Z. Zhou, Y. C. Liou, J. P. Noel, and K. P. Lu. 2002. Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function. J. Biol. Chem. 277:2381-2384.
    • (2002) J. Biol. Chem , vol.277 , pp. 2381-2384
    • Lu, P.J.1    Zhou, X.Z.2    Liou, Y.C.3    Noel, J.P.4    Lu, K.P.5
  • 36
    • 23344441591 scopus 로고    scopus 로고
    • Cross talk in hormonally regulated gene transcription through induction of estrogen receptor ubiquitylation
    • Luo, M., M. Koh, J. Feng, Q. Wu, and P. Melamed. 2005. Cross talk in hormonally regulated gene transcription through induction of estrogen receptor ubiquitylation. Mol. Cell. Biol. 25:7386-7398.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7386-7398
    • Luo, M.1    Koh, M.2    Feng, J.3    Wu, Q.4    Melamed, P.5
  • 37
    • 71849115901 scopus 로고    scopus 로고
    • Melamed, P. 2010. Hormonal signaling to follicle stimulating hormone β-subunit gene expression. Mol. Cell. Endocrinol. 314:204-212.
    • Melamed, P. 2010. Hormonal signaling to follicle stimulating hormone β-subunit gene expression. Mol. Cell. Endocrinol. 314:204-212.
  • 38
    • 0037135610 scopus 로고    scopus 로고
    • Multiple mechanisms for Pitx-1 transactivation of a luteinizing hormone β subunit gene
    • Melamed, P., M. Koh, P. Preklathan, L. Bei, and C. Hew. 2002. Multiple mechanisms for Pitx-1 transactivation of a luteinizing hormone β subunit gene. J. Biol. Chem. 277:26200-26207.
    • (2002) J. Biol. Chem , vol.277 , pp. 26200-26207
    • Melamed, P.1    Koh, M.2    Preklathan, P.3    Bei, L.4    Hew, C.5
  • 39
    • 33745212905 scopus 로고    scopus 로고
    • Transcription of gonadotropin β subunit genes involves cross-talk between the transcription factors and co-regulators that mediate actions of the regulatory hormones
    • Melamed, P., M. N. Abdul Kadir, A. Wijeweera, and S. Seah. 2006. Transcription of gonadotropin β subunit genes involves cross-talk between the transcription factors and co-regulators that mediate actions of the regulatory hormones. Mol. Cell. Endocrinol. 252:167-183.
    • (2006) Mol. Cell. Endocrinol , vol.252 , pp. 167-183
    • Melamed, P.1    Abdul Kadir, M.N.2    Wijeweera, A.3    Seah, S.4
  • 40
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani, M., and W. P. Tansey. 2003. How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol. Cell Biol. 4:192-201.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 42
    • 58049165874 scopus 로고    scopus 로고
    • Signaling by G-protein-coupled receptor (GPCR): Studies on the GnRH receptor
    • Naor, Z. 2009. Signaling by G-protein-coupled receptor (GPCR): studies on the GnRH receptor. Front. Neuroendocrinol. 30:10-29.
    • (2009) Front. Neuroendocrinol , vol.30 , pp. 10-29
    • Naor, Z.1
  • 44
    • 0030218934 scopus 로고    scopus 로고
    • The roles of the nuclear receptor steroidogenic factor 1 in endocrine differentiation and development
    • Parker, K. L., and B. P. Schimmer. 1996. The roles of the nuclear receptor steroidogenic factor 1 in endocrine differentiation and development. Trends Endocrinol. Metab. 7:203-207.
    • (1996) Trends Endocrinol. Metab , vol.7 , pp. 203-207
    • Parker, K.L.1    Schimmer, B.P.2
  • 45
    • 34548706562 scopus 로고    scopus 로고
    • Genotoxic stress regulates expression of the proto-oncogene Bcl6 in germinal center B cells
    • Phan, R. T., M. Saito, Y. Kitagawa, A. R. Means, and R. Dalla-Favera. 2007. Genotoxic stress regulates expression of the proto-oncogene Bcl6 in germinal center B cells. Nat. Immunol. 8:1132-1139.
    • (2007) Nat. Immunol , vol.8 , pp. 1132-1139
    • Phan, R.T.1    Saito, M.2    Kitagawa, Y.3    Means, A.R.4    Dalla-Favera, R.5
  • 46
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart, C. M., and D. Fushman. 2004. Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8:610-616.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 47
    • 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., M. R. Hübner, R. Métivier, H. Brand, S. Denger, D. Manu, J. Beaudouin, J. Ellenberg, and F. Gannon. 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    Hübner, M.R.2    Métivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 49
    • 37549031354 scopus 로고    scopus 로고
    • A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx
    • Ryo, A., A. Hirai, M. Nishi, Y. C. Liou, K. Perrem, S. C. Lin, H. Hirano, S. W. Lee, and I. Aoki. 2007. A suppressive role of the prolyl isomerase Pin1 in cellular apoptosis mediated by the death-associated protein Daxx. J. Biol. Chem. 282:36671-36681.
    • (2007) J. Biol. Chem , vol.282 , pp. 36671-36681
    • Ryo, A.1    Hirai, A.2    Nishi, M.3    Liou, Y.C.4    Perrem, K.5    Lin, S.C.6    Hirano, H.7    Lee, S.W.8    Aoki, I.9
  • 51
    • 0036315162 scopus 로고    scopus 로고
    • Pin1 is an E2F target gene essential for the Neu/Ras-induced transformation of mammary epithelial cells
    • Ryo, A., Y. C. Liou, G. Wulf, M. Nakamura, S. W. Lee, and K. P. Lu. 2002. Pin1 is an E2F target gene essential for the Neu/Ras-induced transformation of mammary epithelial cells. Mol. Cell. Biol. 22:5281-5295.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 5281-5295
    • Ryo, A.1    Liou, Y.C.2    Wulf, G.3    Nakamura, M.4    Lee, S.W.5    Lu, K.P.6
  • 52
    • 13944252067 scopus 로고    scopus 로고
    • The life cycle of C-myc: From synthesis to degradation
    • Sears, R. C. 2004. The life cycle of C-myc: from synthesis to degradation. Cell Cycle 3:1133-1137.
    • (2004) Cell Cycle , vol.3 , pp. 1133-1137
    • Sears, R.C.1
  • 53
    • 33846010183 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and transcription: Is there a twist in the tail? EMBO Rep
    • Shaw, P. E. 2007. Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail? EMBO Rep. 8:40-45.
    • (2007) , vol.8 , pp. 40-45
    • Shaw, P.E.1
  • 54
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80
    • Sims, J. J., and R. E. Cohen. 2009. Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80. Mol. Cell 33:775-783.
    • (2009) Mol. Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 55
    • 0036793173 scopus 로고    scopus 로고
    • Development of a transgenic green fluorescent protein lineage marker for steroidogenic factor 1
    • Stallings, N. R., N. A. Hanley, G. Majdic, L. Zhao, M. Bakke, and K. L. Parker. 2002. Development of a transgenic green fluorescent protein lineage marker for steroidogenic factor 1. Mol. Endocrinol. 16:2360-2370.
    • (2002) Mol. Endocrinol , vol.16 , pp. 2360-2370
    • Stallings, N.R.1    Hanley, N.A.2    Majdic, G.3    Zhao, L.4    Bakke, M.5    Parker, K.L.6
  • 56
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun, L., and Z. J. Chen. 2004. The novel functions of ubiquitination in signaling. Curr. Opin. Cell Biol. 16:119-126.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 57
    • 38949155149 scopus 로고    scopus 로고
    • Prolyl isomerase, Pin1: New findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease
    • Takahashi, K., C. Uchida, R. W. Shin, K. Shimazaki, and T. Uchida. 2008. Prolyl isomerase, Pin1: new findings of post-translational modifications and physiological substrates in cancer, asthma and Alzheimer's disease. Cell. Mol. Life Sci. 65:359-375.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 359-375
    • Takahashi, K.1    Uchida, C.2    Shin, R.W.3    Shimazaki, K.4    Uchida, T.5
  • 58
    • 0033564857 scopus 로고    scopus 로고
    • Ptx1 regulates SF-1 activity by an interaction that mimics the role of the ligand-binding domain
    • Tremblay, J. J., A. Marcil, Y. Gauthier, and J. Drouin. 1999. Ptx1 regulates SF-1 activity by an interaction that mimics the role of the ligand-binding domain. EMBO J. 18:3431-3441.
    • (1999) EMBO J , vol.18 , pp. 3431-3441
    • Tremblay, J.J.1    Marcil, A.2    Gauthier, Y.3    Drouin, J.4
  • 59
    • 0032940188 scopus 로고    scopus 로고
    • Egr-1 is a downstream effector of GnRH and synergizes by direct interaction with Ptx1 and SF-1 to enhance luteinizing hormone β gene transcription
    • Tremblay, J. J., and J. Drouin. 1999. Egr-1 is a downstream effector of GnRH and synergizes by direct interaction with Ptx1 and SF-1 to enhance luteinizing hormone β gene transcription. Mol. Cell. Biol. 19:2567-2576.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 2567-2576
    • Tremblay, J.J.1    Drouin, J.2
  • 60
    • 58849092902 scopus 로고    scopus 로고
    • Proteasome regulation of dynamic transcription factor occupancy on the GnRH-stimulated luteinizing hormone β-subunit promoter
    • Walsh, H. E., and M. A. Shupnik. 2009. Proteasome regulation of dynamic transcription factor occupancy on the GnRH-stimulated luteinizing hormone β-subunit promoter. Mol. Endocrinol. 23:237-250.
    • (2009) Mol. Endocrinol , vol.23 , pp. 237-250
    • Walsh, H.E.1    Shupnik, M.A.2
  • 62
    • 54349112351 scopus 로고    scopus 로고
    • Activator protein-1 and smad proteins synergistically regulate human follicle-stimulating hormone β-promoter activity
    • Wang, Y., J. Fortin, P. Lamba, M. Bonomi, L. Persani, M. S. Roberson, and D. J. Bernard. 2008. Activator protein-1 and smad proteins synergistically regulate human follicle-stimulating hormone β-promoter activity. Endocrinology 149:5577-5591.
    • (2008) Endocrinology , vol.149 , pp. 5577-5591
    • Wang, Y.1    Fortin, J.2    Lamba, P.3    Bonomi, M.4    Persani, L.5    Roberson, M.S.6    Bernard, D.J.7
  • 63
    • 34250001084 scopus 로고    scopus 로고
    • SRC-3 coactivator functional lifetime is regulated by a phospho-dependent ubiquitin time clock
    • Wu, R. C., Q. Feng, D. M. Lonard, and B. W. O'Malley. 2007. SRC-3 coactivator functional lifetime is regulated by a phospho-dependent ubiquitin time clock. Cell 129:1125-1140.
    • (2007) Cell , vol.129 , pp. 1125-1140
    • Wu, R.C.1    Feng, Q.2    Lonard, D.M.3    O'Malley, B.W.4
  • 64
    • 0037230513 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 in breast development and cancer
    • Wulf, G., A. Ryo, Y. C. Liou, and K. P. Lu. 2003. The prolyl isomerase Pin1 in breast development and cancer. Breast Cancer Res. 5:76-82.
    • (2003) Breast Cancer Res , vol.5 , pp. 76-82
    • Wulf, G.1    Ryo, A.2    Liou, Y.C.3    Lu, K.P.4
  • 65
    • 4444309643 scopus 로고    scopus 로고
    • Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis
    • Wulf, G., P. Garg, Y. C. Liou, D. Iglehart, and K. P. Lu. 2004. Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis. EMBO J. 23:3397-3407.
    • (2004) EMBO J , vol.23 , pp. 3397-3407
    • Wulf, G.1    Garg, P.2    Liou, Y.C.3    Iglehart, D.4    Lu, K.P.5
  • 68
    • 33644850537 scopus 로고    scopus 로고
    • The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability
    • Yeh, E. S., B. O. Lew, and A. R. Means. 2006. The loss of PIN1 deregulates cyclin E and sensitizes mouse embryo fibroblasts to genomic instability. J. Biol. Chem. 281:241-251.
    • (2006) J. Biol. Chem , vol.281 , pp. 241-251
    • Yeh, E.S.1    Lew, B.O.2    Means, A.R.3
  • 69
    • 27144480681 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1)
    • Yi, P., R. C. Wu, J. Sandquist, J. Wong, S. Y. Tsai, M. J. Tsai, A. R. Means, and B. W. O'Malley. 2005. Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1). Mol. Cell. Biol. 25:9687-9699.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9687-9699
    • Yi, P.1    Wu, R.C.2    Sandquist, J.3    Wong, J.4    Tsai, S.Y.5    Tsai, M.J.6    Means, A.R.7    O'Malley, B.W.8
  • 70
    • 0036020506 scopus 로고    scopus 로고
    • Pituitary homeobox 1 activates the rat FSHβ (rFSHβ) gene through both direct and indirect interactions with the rFSHβ gene promoter
    • Zakaria, M. M., K. H. Jeong, C. Lacza, and U. B. Kaiser. 2002. Pituitary homeobox 1 activates the rat FSHβ (rFSHβ) gene through both direct and indirect interactions with the rFSHβ gene promoter. Mol. Endocrinol. 16: 1840-1852.
    • (2002) Mol. Endocrinol , vol.16 , pp. 1840-1852
    • Zakaria, M.M.1    Jeong, K.H.2    Lacza, C.3    Kaiser, U.B.4
  • 71
    • 0035924094 scopus 로고    scopus 로고
    • Pituitary-specific knockout of steroidogenic factor 1
    • Zhao, L., M. Bakke, and K. L. Parker. 2001. Pituitary-specific knockout of steroidogenic factor 1. Mol. Cell. Endocrinol. 185:27-32.
    • (2001) Mol. Cell. Endocrinol , vol.185 , pp. 27-32
    • Zhao, L.1    Bakke, M.2    Parker, K.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.