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Volumn 1823, Issue 3, 2012, Pages 722-729

Chaperoning steroidal physiology: Lessons from mouse genetic models of Hsp90 and its cochaperones

Author keywords

FKBP51; FKBP52; Hsp90; P23; Protein phosphatase 5; Steroids

Indexed keywords

ANDROGEN RECEPTOR; CHAPERONE; CYCLOPHILIN; CYCLOPHILIN 40 PROTEIN; ESTROGEN RECEPTOR; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 51; FK 506 BINDING PROTEIN 52; GLUCOCORTICOID; GLUCOCORTICOID RECEPTOR; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90ALPHA; HEAT SHOCK PROTEIN 90BETA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 5; PROGESTERONE RECEPTOR; PROSTAGLANDIN E2; PROTEIN P23; UNCLASSIFIED DRUG;

EID: 84857042430     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.11.006     Document Type: Review
Times cited : (80)

References (100)
  • 1
    • 0022342203 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez E.R., Toft D.O., Schlesinger M.J., Pratt W.B. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 1985, 260:12398-12401.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12398-12401
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 3
    • 0022412314 scopus 로고
    • A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp 60v-src
    • Schuh S., Yonemoto W., Brugge J., Bauer V.J., Riehl R.M., Sullivan W.P., Toft D.O. A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp 60v-src. J. Biol. Chem. 1985, 260:14292-14296.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14292-14296
    • Schuh, S.1    Yonemoto, W.2    Brugge, J.3    Bauer, V.J.4    Riehl, R.M.5    Sullivan, W.P.6    Toft, D.O.7
  • 4
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 1997, 18(3):306-360.
    • (1997) Endocr. Rev. , vol.18 , Issue.3 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 5
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • Picard D. Chaperoning steroid hormone action. Trends Endocrinol. Metab. 2006, 17:229-235.
    • (2006) Trends Endocrinol. Metab. , vol.17 , pp. 229-235
    • Picard, D.1
  • 6
    • 0025260972 scopus 로고
    • In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90
    • Dalman F.C., Koenig R.J., Perdew G.H., Massa E., Pratt W.B. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90. J. Biol. Chem. 1990, 265:3615-3618.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3615-3618
    • Dalman, F.C.1    Koenig, R.J.2    Perdew, G.H.3    Massa, E.4    Pratt, W.B.5
  • 7
    • 0037799205 scopus 로고    scopus 로고
    • Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2
    • Sumanasekera W.K., Tien E.S., Turpey R., Vanden Heuvel J.P., Perdew G.H. Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2. J. Biol. Chem. 2003, 278:4467-4473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4467-4473
    • Sumanasekera, W.K.1    Tien, E.S.2    Turpey, R.3    Vanden Heuvel, J.P.4    Perdew, G.H.5
  • 8
    • 0042318859 scopus 로고    scopus 로고
    • Heat shock protein-90 (Hsp90) acts as a repressor of peroxisome proliferator-activated receptor-alpha (PPARalpha) and PPARbeta activity
    • Sumanasekera W.K., Tien E.S., Davis J.W.n., Turpey R., Perdew G.H., Vanden Heuvel J.P. Heat shock protein-90 (Hsp90) acts as a repressor of peroxisome proliferator-activated receptor-alpha (PPARalpha) and PPARbeta activity. Biochemistry 2003, 42:10726-10735.
    • (2003) Biochemistry , vol.42 , pp. 10726-10735
    • Sumanasekera, W.K.1    Tien, E.S.2    Davis, J.3    Turpey, R.4    Perdew, G.H.5    Vanden Heuvel, J.P.6
  • 9
    • 0031543526 scopus 로고    scopus 로고
    • The Ah receptor is a sensitive target of geldanamycin-induced protein turnover
    • Chen H.S., Singh S.S., Perdew G.H. The Ah receptor is a sensitive target of geldanamycin-induced protein turnover. Arch. Biochem. Biophys. 1997, 348:190-198.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 190-198
    • Chen, H.S.1    Singh, S.S.2    Perdew, G.H.3
  • 10
    • 0042236405 scopus 로고    scopus 로고
    • Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital
    • Yoshinari K., Kobayashi K., Moore R., Kawamoto T., Negishi M. Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital. FEBS Lett. 2003, 548:17-20.
    • (2003) FEBS Lett. , vol.548 , pp. 17-20
    • Yoshinari, K.1    Kobayashi, K.2    Moore, R.3    Kawamoto, T.4    Negishi, M.5
  • 11
    • 8344219885 scopus 로고    scopus 로고
    • Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver
    • Squires E.J., Sueyoshi T., Negishi M. Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver. J. Biol. Chem. 2004, 279:49307-49314.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49307-49314
    • Squires, E.J.1    Sueyoshi, T.2    Negishi, M.3
  • 13
    • 0032924953 scopus 로고    scopus 로고
    • A holding for folding
    • Hsp90 and Co.
    • Buchner J., Hsp90 & Co. A holding for folding. Trends Biochem. Sci. 1999, 24:136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 15
    • 0024567048 scopus 로고
    • Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick E.H., Dalman F.C., Sanchez E.R., Pratt W.B. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 1989, 264:4992-4997.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 16
    • 0025644194 scopus 로고
    • Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex
    • Scherrer L.C., Dalman F.C., Massa E., Meshinchi S., Pratt W.B. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 1990, 265:21397-21400.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21397-21400
    • Scherrer, L.C.1    Dalman, F.C.2    Massa, E.3    Meshinchi, S.4    Pratt, W.B.5
  • 17
    • 0022918191 scopus 로고
    • A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors
    • Tai P.K., Maeda Y., Nakao K., Wakim N.G., Duhring J.L., Faber L.E. A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors. Biochemistry 1986, 25:5269-5275.
    • (1986) Biochemistry , vol.25 , pp. 5269-5275
    • Tai, P.K.1    Maeda, Y.2    Nakao, K.3    Wakim, N.G.4    Duhring, J.L.5    Faber, L.E.6
  • 18
    • 0027219348 scopus 로고
    • Two FKBP-related proteins are associated with progesterone receptor complexes
    • Smith D.F., Baggenstoss B.A., Marion T.N., Rimerman R.A. Two FKBP-related proteins are associated with progesterone receptor complexes. J. Biol. Chem. 1993, 268:18365-18371.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18365-18371
    • Smith, D.F.1    Baggenstoss, B.A.2    Marion, T.N.3    Rimerman, R.A.4
  • 19
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
    • Ratajczak T., Carrello A., Mark P.J., Warner B.J., Simpson R.J., Moritz R.L., House A.K. The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59). J. Biol. Chem. 1993, 268:13187-13192.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.J.3    Warner, B.J.4    Simpson, R.J.5    Moritz, R.L.6    House, A.K.7
  • 20
    • 0029751136 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant
    • Chen M.S., Silverstein A.M., Pratt W.B., Chinkers M. The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant. J. Biol. Chem. 1996, 271:32315-32320.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32315-32320
    • Chen, M.S.1    Silverstein, A.M.2    Pratt, W.B.3    Chinkers, M.4
  • 23
    • 1642268986 scopus 로고    scopus 로고
    • Hsp90 isoforms: functions, expression and clinical importance
    • Sreedhar A.S., Kalmar E., Csermely P., Shen Y.F. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004, 562:11-15.
    • (2004) FEBS Lett. , vol.562 , pp. 11-15
    • Sreedhar, A.S.1    Kalmar, E.2    Csermely, P.3    Shen, Y.F.4
  • 25
    • 39049138736 scopus 로고    scopus 로고
    • A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates
    • Taherian A., Krone P.H., Ovsenek N. A comparison of Hsp90alpha and Hsp90beta interactions with cochaperones and substrates. Biochem. Cell Biol. 2008, 86:37-45.
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 37-45
    • Taherian, A.1    Krone, P.H.2    Ovsenek, N.3
  • 28
    • 0033621681 scopus 로고    scopus 로고
    • Mice lacking HSP90beta fail to develop a placental labyrinth
    • Voss A.K., Thomas T., Gruss P. Mice lacking HSP90beta fail to develop a placental labyrinth. Development 2000, 127:1-11.
    • (2000) Development , vol.127 , pp. 1-11
    • Voss, A.K.1    Thomas, T.2    Gruss, P.3
  • 29
    • 0025233648 scopus 로고
    • Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins
    • Smith D.F., Faber L.E., Toft D.O. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. J. Biol. Chem. 1990, 265:3996-4003.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3996-4003
    • Smith, D.F.1    Faber, L.E.2    Toft, D.O.3
  • 30
    • 0025128697 scopus 로고
    • Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex
    • Bresnick E.H., Dalman F.C., Pratt W.B. Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 1990, 29:520-527.
    • (1990) Biochemistry , vol.29 , pp. 520-527
    • Bresnick, E.H.1    Dalman, F.C.2    Pratt, W.B.3
  • 32
    • 52949139464 scopus 로고    scopus 로고
    • Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions
    • Smith D.F., Toft D.O. Minireview: the intersection of steroid receptors with molecular chaperones: observations and questions. Mol. Endocrinol. 2008, 22(10):2229-2240.
    • (2008) Mol. Endocrinol. , vol.22 , Issue.10 , pp. 2229-2240
    • Smith, D.F.1    Toft, D.O.2
  • 33
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman B.C., Felts S.J., Toft D.O., Yamamoto K.R. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 2000, 14:422-434.
    • (2000) Genes Dev. , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 34
  • 35
    • 33745821260 scopus 로고    scopus 로고
    • The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion
    • Oxelmark E., Roth J.M., Brooks P.C., Braunstein S.E., Schneider R.J., Garabedian M.J. The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion. Mol. Cell. Biol. 2006, 26:5205-5213.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5205-5213
    • Oxelmark, E.1    Roth, J.M.2    Brooks, P.C.3    Braunstein, S.E.4    Schneider, R.J.5    Garabedian, M.J.6
  • 36
    • 0034693050 scopus 로고    scopus 로고
    • Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis
    • Tanioka T., Nakatani Y., Semmyo N., Murakami M., Kudo I. Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis. J. Biol. Chem. 2000, 275:32775-32782.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32775-32782
    • Tanioka, T.1    Nakatani, Y.2    Semmyo, N.3    Murakami, M.4    Kudo, I.5
  • 37
    • 34347249238 scopus 로고    scopus 로고
    • The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation
    • Toogun O.A., Zeiger W., Freeman B.C. The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:5765-5770.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5765-5770
    • Toogun, O.A.1    Zeiger, W.2    Freeman, B.C.3
  • 41
    • 34548281074 scopus 로고    scopus 로고
    • Knockout mice lacking cPGES/p23, a constitutively expressed PGE2 synthetic enzyme, are peri-natally lethal
    • Nakatani Y., Hokonohara Y., Kakuta S., Sudo K., Iwakura Y., Kudo I. Knockout mice lacking cPGES/p23, a constitutively expressed PGE2 synthetic enzyme, are peri-natally lethal. Biochem. Biophys. Res. Commun. 2007, 362:387-392.
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 387-392
    • Nakatani, Y.1    Hokonohara, Y.2    Kakuta, S.3    Sudo, K.4    Iwakura, Y.5    Kudo, I.6
  • 42
    • 34250220325 scopus 로고    scopus 로고
    • CPGES/p23 is required for glucocorticoid receptor function and embryonic growth but not prostaglandin E2 synthesis
    • Lovgren A.K., Kovarova M., Koller B.H. cPGES/p23 is required for glucocorticoid receptor function and embryonic growth but not prostaglandin E2 synthesis. Mol. Cell. Biol. 2007, 27:4416-4430.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4416-4430
    • Lovgren, A.K.1    Kovarova, M.2    Koller, B.H.3
  • 43
    • 79954418920 scopus 로고    scopus 로고
    • Involvement of the constitutive prostaglandin E synthase cPGES/p23 in expression of an initial prostaglandin E2 inactivating enzyme, 15-PGDH
    • Nakatani Y., Hokonohara Y., Tajima Y., Kudo I., Hara S. Involvement of the constitutive prostaglandin E synthase cPGES/p23 in expression of an initial prostaglandin E2 inactivating enzyme, 15-PGDH. Prostaglandins Other Lipid Mediat. 2011, 94:112-117.
    • (2011) Prostaglandins Other Lipid Mediat. , vol.94 , pp. 112-117
    • Nakatani, Y.1    Hokonohara, Y.2    Tajima, Y.3    Kudo, I.4    Hara, S.5
  • 44
    • 34249729416 scopus 로고    scopus 로고
    • Prostaglandin E receptors
    • Sugimoto Y., Narumiya S. Prostaglandin E receptors. J. Biol. Chem. 2007, 282:11613-11617.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11613-11617
    • Sugimoto, Y.1    Narumiya, S.2
  • 48
    • 0021988845 scopus 로고
    • Development of a monoclonal antibody to the rabbit 8.5S uterine progestin receptor
    • Nakao K., Myers J.E., Faber L.E. Development of a monoclonal antibody to the rabbit 8.5S uterine progestin receptor. Can. J. Biochem. Cell Biol. 1985, 63:33-40.
    • (1985) Can. J. Biochem. Cell Biol. , vol.63 , pp. 33-40
    • Nakao, K.1    Myers, J.E.2    Faber, L.E.3
  • 49
    • 0025337581 scopus 로고
    • The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein
    • Renoir J.M., Radanyi C., Faber L.E., Baulieu E.E. The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein. J. Biol. Chem. 1990, 265:10740-10745.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10740-10745
    • Renoir, J.M.1    Radanyi, C.2    Faber, L.E.3    Baulieu, E.E.4
  • 50
    • 0025290187 scopus 로고
    • The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins
    • Sanchez E.R., Faber L.E., Henzel W.J., Pratt W.B. The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry 1990, 29:5145-5152.
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 52
    • 14244262261 scopus 로고    scopus 로고
    • FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
    • Wochnik G.M., Ruegg J., Abel G.A., Schmidt U., Holsboer F., Rein T. FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 2005, 280:4609-4616.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4609-4616
    • Wochnik, G.M.1    Ruegg, J.2    Abel, G.A.3    Schmidt, U.4    Holsboer, F.5    Rein, T.6
  • 53
    • 13544267438 scopus 로고    scopus 로고
    • Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506
    • Davies T.H., Ning Y.M., Sanchez E.R. Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506. Biochemistry 2005, 44:2030-2038.
    • (2005) Biochemistry , vol.44 , pp. 2030-2038
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 55
    • 59849098177 scopus 로고    scopus 로고
    • Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity
    • Wolf I.M., Periyasamy S., Hinds T.D., Yong W., Shou W., Sanchez E.R. Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity. J. Steroid Biochem. Mol. Biol. 2009, 113:36-45.
    • (2009) J. Steroid Biochem. Mol. Biol. , vol.113 , pp. 36-45
    • Wolf, I.M.1    Periyasamy, S.2    Hinds, T.D.3    Yong, W.4    Shou, W.5    Sanchez, E.R.6
  • 56
    • 37549067731 scopus 로고    scopus 로고
    • Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling
    • Riggs D.L., Cox M.B., Tardif H.L., Hessling M., Buchner J., Smith D.F. Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling. Mol. Cell. Biol. 2007, 27:8658-8669.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8658-8669
    • Riggs, D.L.1    Cox, M.B.2    Tardif, H.L.3    Hessling, M.4    Buchner, J.5    Smith, D.F.6
  • 58
    • 76749092246 scopus 로고    scopus 로고
    • The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events
    • Galigniana M.D., Erlejman A.G., Monte M., Gomez-Sanchez C., Piwien-Pilipuk G. The hsp90-FKBP52 complex links the mineralocorticoid receptor to motor proteins and persists bound to the receptor in early nuclear events. Mol. Cell. Biol. 2010, 30:1285-1298.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1285-1298
    • Galigniana, M.D.1    Erlejman, A.G.2    Monte, M.3    Gomez-Sanchez, C.4    Piwien-Pilipuk, G.5
  • 59
    • 52949129878 scopus 로고    scopus 로고
    • Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins
    • Banerjee A., Periyasamy S., Wolf I.M., Hinds T.D.J., Yong W., Shou W., Sanchez E.R. Control of glucocorticoid and progesterone receptor subcellular localization by the ligand-binding domain is mediated by distinct interactions with tetratricopeptide repeat proteins. Biochemistry 2008, 47:10471-10480.
    • (2008) Biochemistry , vol.47 , pp. 10471-10480
    • Banerjee, A.1    Periyasamy, S.2    Wolf, I.M.3    Hinds, T.D.J.4    Yong, W.5    Shou, W.6    Sanchez, E.R.7
  • 62
    • 77956234689 scopus 로고    scopus 로고
    • Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis
    • Chen H., Yong W., Hinds T.D.J., Yang Z., Zhou Y., Sanchez E.R., Shou W. Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis. J. Biol. Chem. 2010, 285:27776-27784.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27776-27784
    • Chen, H.1    Yong, W.2    Hinds, T.D.J.3    Yang, Z.4    Zhou, Y.5    Sanchez, E.R.6    Shou, W.7
  • 64
    • 34447122476 scopus 로고    scopus 로고
    • FKBP52 deficiency-conferred uterine progesterone resistance is genetic background and pregnancy stage specific
    • Tranguch S., Wang H., Daikoku T., Xie H., Smith D.F., Dey S.K. FKBP52 deficiency-conferred uterine progesterone resistance is genetic background and pregnancy stage specific. J. Clin. Invest. 2007, 117:1824-1834.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1824-1834
    • Tranguch, S.1    Wang, H.2    Daikoku, T.3    Xie, H.4    Smith, D.F.5    Dey, S.K.6
  • 67
    • 80051667737 scopus 로고    scopus 로고
    • FKBP51-a selective modulator of glucocorticoid and androgen sensitivity
    • Stechschulte L.A., Sanchez E.R. FKBP51-a selective modulator of glucocorticoid and androgen sensitivity. Curr. Opin. Pharmacol. 2011, 11:332-337.
    • (2011) Curr. Opin. Pharmacol. , vol.11 , pp. 332-337
    • Stechschulte, L.A.1    Sanchez, E.R.2
  • 68
    • 0037900196 scopus 로고    scopus 로고
    • The FK506-binding immunophilin FKBP51 is transcriptionally regulated by progestin and attenuates progestin responsiveness
    • Hubler T.R., Denny W.B., Valentine D.L., Cheung-Flynn J., Smith D.F., Scammell J.G. The FK506-binding immunophilin FKBP51 is transcriptionally regulated by progestin and attenuates progestin responsiveness. Endocrinology 2003, 144:2380-2387.
    • (2003) Endocrinology , vol.144 , pp. 2380-2387
    • Hubler, T.R.1    Denny, W.B.2    Valentine, D.L.3    Cheung-Flynn, J.4    Smith, D.F.5    Scammell, J.G.6
  • 69
    • 17144370286 scopus 로고    scopus 로고
    • Androgen mediated regulation and functional implications of fkbp51 expression in prostate cancer
    • Febbo P.G., Lowenberg M., Thorner A.R., Brown M., Loda M., Golub T.R. Androgen mediated regulation and functional implications of fkbp51 expression in prostate cancer. J. Urol. 2005, 173:1772-1777.
    • (2005) J. Urol. , vol.173 , pp. 1772-1777
    • Febbo, P.G.1    Lowenberg, M.2    Thorner, A.R.3    Brown, M.4    Loda, M.5    Golub, T.R.6
  • 70
    • 76749108107 scopus 로고    scopus 로고
    • FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells
    • Ni L., Yang C.S., Gioeli D., Frierson H., Toft D.O., Paschal B.M. FKBP51 promotes assembly of the Hsp90 chaperone complex and regulates androgen receptor signaling in prostate cancer cells. Mol. Cell. Biol. 2010, 30:1243-1253.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1243-1253
    • Ni, L.1    Yang, C.S.2    Gioeli, D.3    Frierson, H.4    Toft, D.O.5    Paschal, B.M.6
  • 71
    • 77949654801 scopus 로고    scopus 로고
    • FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A
    • Periyasamy S., Hinds T.J., Shemshedini L., Shou W., Sanchez E.R. FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A. Oncogene 2010, 29:1691-1701.
    • (2010) Oncogene , vol.29 , pp. 1691-1701
    • Periyasamy, S.1    Hinds, T.J.2    Shemshedini, L.3    Shou, W.4    Sanchez, E.R.5
  • 72
    • 0034812087 scopus 로고    scopus 로고
    • Silymarin inhibits function of the androgen receptor by reducing nuclear localization of the receptor in the human prostate cancer cell line LNCaP
    • Zhu W., Zhang J.S., Young C.Y. Silymarin inhibits function of the androgen receptor by reducing nuclear localization of the receptor in the human prostate cancer cell line LNCaP. Carcinogenesis 2001, 22:1399-1403.
    • (2001) Carcinogenesis , vol.22 , pp. 1399-1403
    • Zhu, W.1    Zhang, J.S.2    Young, C.Y.3
  • 76
    • 29344467436 scopus 로고    scopus 로고
    • Direct, androgen receptor-mediated regulation of the FKBP5 gene via a distal enhancer element
    • Magee J.A., Chang L.W., Stormo G.D., Milbrandt J. Direct, androgen receptor-mediated regulation of the FKBP5 gene via a distal enhancer element. Endocrinology 2006, 147:590-598.
    • (2006) Endocrinology , vol.147 , pp. 590-598
    • Magee, J.A.1    Chang, L.W.2    Stormo, G.D.3    Milbrandt, J.4
  • 77
    • 67651180792 scopus 로고    scopus 로고
    • Long-range activation of FKBP51 transcription by the androgen receptor via distal intronic enhancers
    • Makkonen H., Kauhanen M., Paakinaho V., Jaaskelainen T., Palvimo J.J. Long-range activation of FKBP51 transcription by the androgen receptor via distal intronic enhancers. Nucleic Acids Res. 2009, 37:4135-4148.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4135-4148
    • Makkonen, H.1    Kauhanen, M.2    Paakinaho, V.3    Jaaskelainen, T.4    Palvimo, J.J.5
  • 79
    • 65549122835 scopus 로고    scopus 로고
    • Pharmacogenetics of antidepressant response: an update
    • Drago A., De Ronchi D., Serretti A. Pharmacogenetics of antidepressant response: an update. Hum. Genomics 2009, 3:257-274.
    • (2009) Hum. Genomics , vol.3 , pp. 257-274
    • Drago, A.1    De Ronchi, D.2    Serretti, A.3
  • 86
    • 0033913213 scopus 로고    scopus 로고
    • Signaling pathways in insulin action: molecular targets of insulin resistance
    • Pessin J.E., Saltiel A.R. Signaling pathways in insulin action: molecular targets of insulin resistance. J. Clin. Invest. 2000, 106:165-169.
    • (2000) J. Clin. Invest. , vol.106 , pp. 165-169
    • Pessin, J.E.1    Saltiel, A.R.2
  • 88
    • 43049097815 scopus 로고    scopus 로고
    • The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer
    • Golden T., Swingle M., Honkanen R.E. The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer. Cancer Metastasis Rev. 2008, 27:169-178.
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 169-178
    • Golden, T.1    Swingle, M.2    Honkanen, R.E.3
  • 89
    • 34447525646 scopus 로고    scopus 로고
    • Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest
    • Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W. Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia mutated (ATM)-mediated cell cycle arrest. J. Biol. Chem. 2007, 282:14690-14694.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14690-14694
    • Yong, W.1    Bao, S.2    Chen, H.3    Li, D.4    Sanchez, E.R.5    Shou, W.6
  • 91
    • 0035920229 scopus 로고    scopus 로고
    • Identification of an estrogen-inducible phosphatase (PP5) that converts MCF-7 human breast carcinoma cells into an estrogen-independent phenotype when expressed constitutively
    • Urban G., Golden T., Aragon I.V., Scammell J.G., Dean N.M., Honkanen R.E. Identification of an estrogen-inducible phosphatase (PP5) that converts MCF-7 human breast carcinoma cells into an estrogen-independent phenotype when expressed constitutively. J. Biol. Chem. 2001, 276:27638-27646.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27638-27646
    • Urban, G.1    Golden, T.2    Aragon, I.V.3    Scammell, J.G.4    Dean, N.M.5    Honkanen, R.E.6
  • 92
    • 0038660681 scopus 로고    scopus 로고
    • Identification of a functional link for the p53 tumor suppressor protein in dexamethasone-induced growth suppression
    • Urban G., Golden T., Aragon I.V., Cowsert L., Cooper S.R., Dean N.M., Honkanen R.E. Identification of a functional link for the p53 tumor suppressor protein in dexamethasone-induced growth suppression. J. Biol. Chem. 2003, 278:9747-9753.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9747-9753
    • Urban, G.1    Golden, T.2    Aragon, I.V.3    Cowsert, L.4    Cooper, S.R.5    Dean, N.M.6    Honkanen, R.E.7
  • 93
    • 69949173906 scopus 로고    scopus 로고
    • Estrogen inhibits glucocorticoid action via protein phosphatase 5 (PP5) mediated glucocorticoid receptor dephosphorylation
    • Zhang Y., Leung D.Y., Nordeen S.K., Goleva E. Estrogen inhibits glucocorticoid action via protein phosphatase 5 (PP5) mediated glucocorticoid receptor dephosphorylation. J. Biol. Chem. 2009.
    • (2009) J. Biol. Chem.
    • Zhang, Y.1    Leung, D.Y.2    Nordeen, S.K.3    Goleva, E.4
  • 94
    • 4544233003 scopus 로고    scopus 로고
    • Constitutive over expression of serine/threonine protein phosphatase 5 (PP5) augments estrogen-dependent tumor growth in mice
    • Golden T., Aragon I.V., Zhou G., Cooper S.R., Dean N.M., Honkanen R.E. Constitutive over expression of serine/threonine protein phosphatase 5 (PP5) augments estrogen-dependent tumor growth in mice. Cancer Lett. 2004, 215:95-100.
    • (2004) Cancer Lett. , vol.215 , pp. 95-100
    • Golden, T.1    Aragon, I.V.2    Zhou, G.3    Cooper, S.R.4    Dean, N.M.5    Honkanen, R.E.6
  • 96
    • 0031015069 scopus 로고    scopus 로고
    • Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain
    • Chen M.X., Cohen P.T. Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain. FEBS Lett. 1997, 400:136-140.
    • (1997) FEBS Lett. , vol.400 , pp. 136-140
    • Chen, M.X.1    Cohen, P.T.2
  • 97
    • 0030928118 scopus 로고    scopus 로고
    • Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5
    • Skinner J., Sinclair C., Romeo C., Armstrong D., Charbonneau H., Rossie S. Purification of a fatty acid-stimulated protein-serine/threonine phosphatase from bovine brain and its identification as a homolog of protein phosphatase 5. J. Biol. Chem. 1997, 272:22464-22471.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22464-22471
    • Skinner, J.1    Sinclair, C.2    Romeo, C.3    Armstrong, D.4    Charbonneau, H.5    Rossie, S.6
  • 98
    • 0035807022 scopus 로고    scopus 로고
    • Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation
    • Kang H., Sayner S.L., Gross K.L., Russell L.C., Chinkers M. Identification of amino acids in the tetratricopeptide repeat and C-terminal domains of protein phosphatase 5 involved in autoinhibition and lipid activation. Biochemistry 2001, 40:10485-10490.
    • (2001) Biochemistry , vol.40 , pp. 10485-10490
    • Kang, H.1    Sayner, S.L.2    Gross, K.L.3    Russell, L.C.4    Chinkers, M.5
  • 99
    • 79959581081 scopus 로고    scopus 로고
    • Extra-adrenal glucocorticoids and mineralocorticoids: evidence for local synthesis, regulation, and function
    • Taves M.D., Gomez-Sanchez C.E., Soma K.K. Extra-adrenal glucocorticoids and mineralocorticoids: evidence for local synthesis, regulation, and function. Am. J. Physiol. Endocrinol. Metab. 2011, 301:E11-E24.
    • (2011) Am. J. Physiol. Endocrinol. Metab. , vol.301
    • Taves, M.D.1    Gomez-Sanchez, C.E.2    Soma, K.K.3


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