메뉴 건너뛰기




Volumn 30, Issue 1, 2010, Pages 220-230

Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE P38; STEROID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 73549096417     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00552-09     Document Type: Article
Times cited : (90)

References (45)
  • 1
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade, M.A., P. Chacón, J. J. Merelo, and F. Morán. 1993. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Protein Eng. 6:383-390.
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 2
    • 0037385141 scopus 로고    scopus 로고
    • Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells
    • Bai, Y., and V. Giguére. 2003. Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells. Mol. Endocrinol. 17:589-599.
    • (2003) Mol. Endocrinol , vol.17 , pp. 589-599
    • Bai, Y.1    Giguére, V.2
  • 3
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin, R. L., and G. D. Rose. 1999. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24:77-83.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 4
    • 0344527724 scopus 로고    scopus 로고
    • Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor
    • Baskakov, I. V., R. Kumar, G. Srinivasan, Y. Ji, D. W. Bolen, and E. B. Thompson. 1999. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. J. Biol. Chem. 274:10693-10696.
    • (1999) J. Biol. Chem , vol.274 , pp. 10693-10696
    • Baskakov, I.V.1    Kumar, R.2    Srinivasan, G.3    Ji, Y.4    Bolen, D.W.5    Thompson, E.B.6
  • 5
    • 40849102229 scopus 로고    scopus 로고
    • Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes
    • Blind, R. D., and M. J. Garabedian. 2008. Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes. J. Steroid Biochem. Mol. Biol. 109:150-157.
    • (2008) J. Steroid Biochem. Mol. Biol , vol.109 , pp. 150-157
    • Blind, R.D.1    Garabedian, M.J.2
  • 6
    • 0027742105 scopus 로고
    • Glucocorticoid receptors: ATP-dependent cycling and hormone-dependent hyper-phosphorylation
    • Bodwell, J. E., L. M. Hu, J. M. Hu, E. Ortí, and A. Munck. 1993. Glucocorticoid receptors: ATP-dependent cycling and hormone-dependent hyper-phosphorylation. J. Steroid Biochem. Mol. Biol. 47:31-38.
    • (1993) J. Steroid Biochem. Mol. Biol , vol.47 , pp. 31-38
    • Bodwell, J.E.1    Hu, L.M.2    Hu, J.M.3    Ortí, E.4    Munck, A.5
  • 9
    • 33748579587 scopus 로고    scopus 로고
    • Alternative O-GlcNAcylation/O-phosphorylation of Ser16 induce different conformational Disturbances to the N terminus of murine estrogen receptor β
    • Chen, Y. X., J. T. Du, L. X. Zhou, X. H. Liu, Y. F. Zhao, H. Nakanishi, and Y. M. Li. 2006. Alternative O-GlcNAcylation/O-phosphorylation of Ser16 induce different conformational Disturbances to the N terminus of murine estrogen receptor β. Chem. Biol. 13:937-944.
    • (2006) Chem. Biol , vol.13 , pp. 937-944
    • Chen, Y.X.1    Du, J.T.2    Zhou, L.X.3    Liu, X.H.4    Zhao, Y.F.5    Nakanishi, H.6    Li, Y.M.7
  • 10
    • 0024269449 scopus 로고    scopus 로고
    • Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptor
    • Dalman, F. C., E. R. Sanchez, A. L. Lin, F. Perini, and W. B. Pratt. 1998. Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptor. J. Biol. Chem. 263:12259-12267.
    • (1998) J. Biol. Chem , vol.263 , pp. 12259-12267
    • Dalman, F.C.1    Sanchez, E.R.2    Lin, A.L.3    Perini, F.4    Pratt, W.B.5
  • 11
    • 0026406078 scopus 로고
    • Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors
    • DeFranco, D. B., M. Qi, K. C. Borror, M. J. Garabedian, and D. L. Brautigan. 1991. Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Mol. Endocrinol. 5:1215-1228.
    • (1991) Mol. Endocrinol , vol.5 , pp. 1215-1228
    • DeFranco, D.B.1    Qi, M.2    Borror, K.C.3    Garabedian, M.J.4    Brautigan, D.L.5
  • 12
    • 0026557269 scopus 로고
    • Transcriptional transactivation functions localized to the glucocorticoid receptor N terminus are necessary for steroid induction of lymphocyte apoptosis
    • Dieken, E. S., and R. L. Miesfeld. 1992. Transcriptional transactivation functions localized to the glucocorticoid receptor N terminus are necessary for steroid induction of lymphocyte apoptosis. Mol. Cell. Biol. 12:589-597.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 589-597
    • Dieken, E.S.1    Miesfeld, R.L.2
  • 14
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker, A. K., and V. N. Uversky. 2008. Signal transduction via unstructured protein conduits. Nat. Chem. Biol. 4:229-230.
    • (2008) Nat. Chem. Biol , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 15
    • 0023150589 scopus 로고
    • Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
    • Godowski, P. J., S. Rusconi, R. L. Miesfeld, and K. R. Yamamoto. 1987. Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement. Nature 325:365-368.
    • (1987) Nature , vol.325 , pp. 365-368
    • Godowski, P.J.1    Rusconi, S.2    Miesfeld, R.L.3    Yamamoto, K.R.4
  • 16
    • 0025190888 scopus 로고
    • Reduced DNA flexibility in complexes with a type II DNA binding protein
    • Härd, T., and D. R. Kearns. 1990. Reduced DNA flexibility in complexes with a type II DNA binding protein. Biochemistry 29:959-965.
    • (1990) Biochemistry , vol.29 , pp. 959-965
    • Härd, T.1    Kearns, D.R.2
  • 17
    • 0034726060 scopus 로고    scopus 로고
    • Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains
    • Hay, T. J., and D. W. Meek. 2000. Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains. FEBS Lett. 478:183-186.
    • (2000) FEBS Lett , vol.478 , pp. 183-186
    • Hay, T.J.1    Meek, D.W.2
  • 19
    • 0034731505 scopus 로고    scopus 로고
    • p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1)
    • King, C. C., E. M. Gardiner, F. T. Zenke, B. P. Bohl, A. C. Newton, B. A. Hemmings, and G. M. Bokoch. 2000. p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). J. Biol. Chem. 275: 41201-41209.
    • (2000) J. Biol. Chem , vol.275 , pp. 41201-41209
    • King, C.C.1    Gardiner, E.M.2    Zenke, F.T.3    Bohl, B.P.4    Newton, A.C.5    Hemmings, B.A.6    Bokoch, G.M.7
  • 20
    • 18144424777 scopus 로고    scopus 로고
    • Gene regulation by the glucocorticoid receptor: Structure:function relationship
    • Kumar, R., and E. B. Thompson. 2005. Gene regulation by the glucocorticoid receptor: structure:function relationship. J. Steroid Biochem. Mol. Biol. 94:383-394.
    • (2005) J. Steroid Biochem. Mol. Biol , vol.94 , pp. 383-394
    • Kumar, R.1    Thompson, E.B.2
  • 21
    • 34548396816 scopus 로고    scopus 로고
    • Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor
    • Kumar, R., J. M. Serrette, S. H. Khan, A. L. Miller, and E. B. Thompson. 2007. Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor. Arch. Biochem. Biophys. 465:452-460.
    • (2007) Arch. Biochem. Biophys , vol.465 , pp. 452-460
    • Kumar, R.1    Serrette, J.M.2    Khan, S.H.3    Miller, A.L.4    Thompson, E.B.5
  • 22
    • 0035947672 scopus 로고    scopus 로고
    • The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins
    • Kumar, R., J. C. Lee, D. W. Bolen, and E. B. Thompson. 2001. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. J. Biol. Chem. 276:18146-18152.
    • (2001) J. Biol. Chem , vol.276 , pp. 18146-18152
    • Kumar, R.1    Lee, J.C.2    Bolen, D.W.3    Thompson, E.B.4
  • 23
    • 1542743970 scopus 로고    scopus 로고
    • Induced α-helix structure in AF1 of androgen receptor upon binding transcription factor TFIIF
    • Kumar, R., R. Betney, J. Li, E. B. Thompson, and I. J. McEwan. 2004. Induced α-helix structure in AF1 of androgen receptor upon binding transcription factor TFIIF. Biochemistry 43:3008-3013.
    • (2004) Biochemistry , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.B.4    McEwan, I.J.5
  • 24
    • 3142716735 scopus 로고    scopus 로고
    • Overview of the structural basis for transcription regulation by nuclear hormone receptors
    • Kumar, R., B. H. Johnson, and E. B. Thompson. 2004. Overview of the structural basis for transcription regulation by nuclear hormone receptors. Essays Biochem. 40:27-39.
    • (2004) Essays Biochem , vol.40 , pp. 27-39
    • Kumar, R.1    Johnson, B.H.2    Thompson, E.B.3
  • 25
    • 9344227341 scopus 로고    scopus 로고
    • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar, R., D. E. Volk, J. Li, J. C. Lee, D. W. Gorenstein, and E. B. Thompson. 2004. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc. Natl. Acad. Sci. USA 101:16425-16430.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.E.2    Li, J.3    Lee, J.C.4    Gorenstein, D.W.5    Thompson, E.B.6
  • 26
    • 0021274536 scopus 로고
    • Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase
    • Kurl, R. N., and S. T. Jacob. 1984. Phosphorylation of purified glucocorticoid receptor from rat liver by an endogenous protein kinase. Biochem. Biophys. Res. Commun. 119:700-705.
    • (1984) Biochem. Biophys. Res. Commun , vol.119 , pp. 700-705
    • Kurl, R.N.1    Jacob, S.T.2
  • 27
    • 0034609368 scopus 로고    scopus 로고
    • MAP kinases and the regulation of nuclear receptors
    • Kyriakis, J. M. 2000. MAP kinases and the regulation of nuclear receptors. Sci. STKE PE1.
    • (2000) Sci. STKE
    • Kyriakis, J.M.1
  • 28
    • 27744511919 scopus 로고    scopus 로고
    • Structure and function of steroid receptor AF1 transactivation domains: Induction of active conformations
    • Lavery, D. N., and I. J. McEwan. 2005. Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations. Biochem. J. 391:449-464.
    • (2005) Biochem. J , vol.391 , pp. 449-464
    • Lavery, D.N.1    McEwan, I.J.2
  • 31
    • 0029740873 scopus 로고    scopus 로고
    • Functional interaction of the c-Myc transactivation domain with the TATA binding protein: Evidence for an induced fit model of transactivation domain folding
    • McEwan, I. J., K. Dahlman-Wright, J. Ford, and A. P. Wright. 1996. Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. Biochemistry 35:9584-9593.
    • (1996) Biochemistry , vol.35 , pp. 9584-9593
    • McEwan, I.J.1    Dahlman-Wright, K.2    Ford, J.3    Wright, A.P.4
  • 33
    • 22344458207 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: Correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211
    • Miller, A. L., M. S. Webb, A. J. Copik, Y. Wang, B. H. Johnson, R. Kumar, and E. B. Thompson. 2005. p38 mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol. Endocrinol. 19:1569-1583.
    • (2005) Mol. Endocrinol , vol.19 , pp. 1569-1583
    • Miller, A.L.1    Webb, M.S.2    Copik, A.J.3    Wang, Y.4    Johnson, B.H.5    Kumar, R.6    Thompson, E.B.7
  • 34
    • 34247209568 scopus 로고    scopus 로고
    • Pathway interactions between MAPKs, mTOR, PKA, and the glucocorticoid receptor in lymphoid cells
    • Miller, A. L., A. S. Garza, B. H. Johnson, and E. B. Thompson. 2007. Pathway interactions between MAPKs, mTOR, PKA, and the glucocorticoid receptor in lymphoid cells. Cancer Cell Int. 7:3.
    • (2007) Cancer Cell Int , vol.7 , pp. 3
    • Miller, A.L.1    Garza, A.S.2    Johnson, B.H.3    Thompson, E.B.4
  • 35
    • 33744829805 scopus 로고    scopus 로고
    • Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation
    • Minezaki, Y., K. Homma, A. R. Kinjo, and K. Nishikawa. 2006. Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation. J. Mol. Biol. 359:1137-1149.
    • (2006) J. Mol. Biol , vol.359 , pp. 1137-1149
    • Minezaki, Y.1    Homma, K.2    Kinjo, A.R.3    Nishikawa, K.4
  • 37
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 38
    • 0032478254 scopus 로고    scopus 로고
    • Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
    • Rogatsky, I., S. K. Logan, and M. J. Garabedian. 1998. Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase. Proc. Natl. Acad. Sci. USA 95:2050-2055.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2050-2055
    • Rogatsky, I.1    Logan, S.K.2    Garabedian, M.J.3
  • 39
    • 0032486406 scopus 로고    scopus 로고
    • Phosphorylation and inhibition of rat glucocorticoid receptor transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-specific differences between human and rat glucocorticoid receptor signaling as revealed through GSK-3 phosphorylation
    • Rogatsky, I., C. L. Waase, and J. M. Garabedian. 1998. Phosphorylation and inhibition of rat glucocorticoid receptor transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-specific differences between human and rat glucocorticoid receptor signaling as revealed through GSK-3 phosphorylation. J. Biol. Chem. 273:14315-14321.
    • (1998) J. Biol. Chem , vol.273 , pp. 14315-14321
    • Rogatsky, I.1    Waase, C.L.2    Garabedian, J.M.3
  • 40
    • 0034833014 scopus 로고    scopus 로고
    • Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1
    • Vetter, S. W., and E. Leclerc. 2001. Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1. Eur. J. Biochem. 268:4292-4299.
    • (2001) Eur. J. Biochem , vol.268 , pp. 4292-4299
    • Vetter, S.W.1    Leclerc, E.2
  • 41
    • 2342562556 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in apoptosis regulation
    • Wada, T., and J. M. Penninger. 2004. Mitogen-activated protein kinases in apoptosis regulation. Oncogene 23:2838-2849.
    • (2004) Oncogene , vol.23 , pp. 2838-2849
    • Wada, T.1    Penninger, J.M.2
  • 42
    • 0037135596 scopus 로고    scopus 로고
    • Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo
    • Wang, Z., J. Frederick, and M. J. Garabedian. 2002. Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo. J. Biol. Chem. 277:26573-26580.
    • (2002) J. Biol. Chem , vol.277 , pp. 26573-26580
    • Wang, Z.1    Frederick, J.2    Garabedian, M.J.3
  • 43
    • 0030900729 scopus 로고    scopus 로고
    • Mouse glucocorticoid receptor phosphorylation status in-fluences multiple functions of the receptor protein
    • Webster, J. C., C. M. Jewell, M. Sar, J. E. Bodwell, A. Munck, and J. A. Cidlowski. 1997. Mouse glucocorticoid receptor phosphorylation status in-fluences multiple functions of the receptor protein. J. Biol. Chem. 272:9287-9293.
    • (1997) J. Biol. Chem , vol.272 , pp. 9287-9293
    • Webster, J.C.1    Jewell, C.M.2    Sar, M.3    Bodwell, J.E.4    Munck, A.5    Cidlowski, J.A.6
  • 44
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke, F. T., C. C. King, B. P. Bohl, and G. M. Bokoch. 1999. Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J. Biol. Chem. 274:32565-32573.
    • (1999) J. Biol. Chem , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4
  • 45
    • 0036829096 scopus 로고    scopus 로고
    • Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    • Zor, T., B. M. Mayr, H. J. Dyson, M. R. Montminy, and P. E. Wright. 2002. Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J. Biol. Chem. 277:42241-42248.
    • (2002) J. Biol. Chem , vol.277 , pp. 42241-42248
    • Zor, T.1    Mayr, B.M.2    Dyson, H.J.3    Montminy, M.R.4    Wright, P.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.