메뉴 건너뛰기




Volumn 102, Issue 4, 2007, Pages 1021-1035

RIF-1, a novel nuclear receptor corepressor that associates with the nuclear matrix

Author keywords

Corepressor; Nuclear matrix protein; Nuclear receptor; Transcription

Indexed keywords

CELL NUCLEUS RECEPTOR; PROTEIN; PROTEIN RIF 1; REPRESSOR PROTEIN; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR ALPHA; UNCLASSIFIED DRUG;

EID: 35648993041     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.21340     Document Type: Article
Times cited : (20)

References (56)
  • 1
    • 0030959244 scopus 로고    scopus 로고
    • Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression [see comments]
    • Alland L, Muhle R, Hou H, Jr., Potes J, Chin L, Schreiber-Agus N, DePinho RA. 1997. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression [see comments]. Nature 387:49-55.
    • (1997) Nature , vol.387 , pp. 49-55
    • Alland, L.1    Muhle, R.2    Hou Jr., H.3    Potes, J.4    Chin, L.5    Schreiber-Agus, N.6    DePinho, R.A.7
  • 2
    • 2942620522 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Their modification codes and regulatory mechanism by translocation
    • Baek SH, Rosenfeld MG. 2004. Nuclear receptor coregulators: Their modification codes and regulatory mechanism by translocation. Biochem Biophys Res Commun 319:707-714.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 707-714
    • Baek, S.H.1    Rosenfeld, M.G.2
  • 3
    • 0032608965 scopus 로고    scopus 로고
    • Nuclear matrix and steroid hormone action
    • Barrett TJ, Spelsberg TC. 1999. Nuclear matrix and steroid hormone action. Vitam Horm 55:127-163.
    • (1999) Vitam Horm , vol.55 , pp. 127-163
    • Barrett, T.J.1    Spelsberg, T.C.2
  • 4
    • 0034103927 scopus 로고    scopus 로고
    • Transcriptional augmentation: Modulation of gene expression by scaffold/matrix-attached regions (S/MAR elements)
    • Bode J, Benham C, Knopp A, Mielke C. 2000. Transcriptional augmentation: Modulation of gene expression by scaffold/matrix-attached regions (S/MAR elements). Crit Rev Eukaryot Gene Expr 10:73-90.
    • (2000) Crit Rev Eukaryot Gene Expr , vol.10 , pp. 73-90
    • Bode, J.1    Benham, C.2    Knopp, A.3    Mielke, C.4
  • 6
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors [see comments]
    • Chen JD, Evans RM. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors [see comments]. Nature 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 7
    • 0029794881 scopus 로고    scopus 로고
    • SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers
    • Chen JD, Umesono K, Evans RM. 1996. SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers. Proc Natl Acad Sci USA 93:7567-7571.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7567-7571
    • Chen, J.D.1    Umesono, K.2    Evans, R.M.3
  • 9
    • 29744437121 scopus 로고    scopus 로고
    • Scaffold attachment factor B1 directly interacts with nuclear receptors in living cells and represses transcriptional activity
    • Debril MB, Dubuquoy L, Feige JN, Wahli W, Desvergne B, Auwerx J, Gelman L. 2005. Scaffold attachment factor B1 directly interacts with nuclear receptors in living cells and represses transcriptional activity. J Mol Endocrinol 35:503-517.
    • (2005) J Mol Endocrinol , vol.35 , pp. 503-517
    • Debril, M.B.1    Dubuquoy, L.2    Feige, J.N.3    Wahli, W.4    Desvergne, B.5    Auwerx, J.6    Gelman, L.7
  • 10
    • 0034103267 scopus 로고    scopus 로고
    • Nuclear matrix targeting of steroid receptors: Specific signal sequences and acceptor proteins
    • DeFranco DB, Guerrero J. 2000. Nuclear matrix targeting of steroid receptors: Specific signal sequences and acceptor proteins. Crit Rev Eukaryot Gene Expr 10:39-44.
    • (2000) Crit Rev Eukaryot Gene Expr , vol.10 , pp. 39-44
    • DeFranco, D.B.1    Guerrero, J.2
  • 11
    • 0034680931 scopus 로고    scopus 로고
    • Analysis of estrogen receptor interaction with a repressor of estrogen receptor activity (REA) and the regulation of estrogen receptor transcriptional activity by REA
    • Delage-Mourroux R, Martini PG, Choi I, Kraichely DM, Hoeksema J, Katzenellenbogen BS. 2000. Analysis of estrogen receptor interaction with a repressor of estrogen receptor activity (REA) and the regulation of estrogen receptor transcriptional activity by REA. J Biol Chem 275:35848-35856.
    • (2000) J Biol Chem , vol.275 , pp. 35848-35856
    • Delage-Mourroux, R.1    Martini, P.G.2    Choi, I.3    Kraichely, D.M.4    Hoeksema, J.5    Katzenellenbogen, B.S.6
  • 14
    • 0141785350 scopus 로고    scopus 로고
    • Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: Insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype
    • Frasor J, Danes JM, Komm B, Chang KC, Lyttle CR, Katzenellenbogen BS. 2003. Profiling of estrogen up- and down-regulated gene expression in human breast cancer cells: Insights into gene networks and pathways underlying estrogenic control of proliferation and cell phenotype. Endocrinology 144:4562-4574.
    • (2003) Endocrinology , vol.144 , pp. 4562-4574
    • Frasor, J.1    Danes, J.M.2    Komm, B.3    Chang, K.C.4    Lyttle, C.R.5    Katzenellenbogen, B.S.6
  • 15
    • 25444521520 scopus 로고    scopus 로고
    • Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha
    • Georgescu SP, Li JH, Lu Q, Karas RH, Brown M, Mendelsohn ME. 2005. Modulator recognition factor 1, an AT-rich interaction domain family member, is a novel corepressor for estrogen receptor alpha. Mol Endocrinol 19:2491-2501.
    • (2005) Mol Endocrinol , vol.19 , pp. 2491-2501
    • Georgescu, S.P.1    Li, J.H.2    Lu, Q.3    Karas, R.H.4    Brown, M.5    Mendelsohn, M.E.6
  • 19
    • 23444434548 scopus 로고    scopus 로고
    • Nuclear hormone receptor degradation and gene transcription: An update
    • Ismail A, Nawaz Z. 2005. Nuclear hormone receptor degradation and gene transcription: An update. IUBMB Life 57:483-490.
    • (2005) IUBMB Life , vol.57 , pp. 483-490
    • Ismail, A.1    Nawaz, Z.2
  • 21
    • 31444449277 scopus 로고    scopus 로고
    • Scaffold attachment factor SAFB1 suppresses estrogen receptor alpha-mediated transcription in part via interaction with nuclear receptor corepressor
    • Jiang S, Meyer R, Kang K, Osborne CK, Wong J, Oesterreich S. 2006. Scaffold attachment factor SAFB1 suppresses estrogen receptor alpha-mediated transcription in part via interaction with nuclear receptor corepressor. Mol Endocrinol 20:311-320.
    • (2006) Mol Endocrinol , vol.20 , pp. 311-320
    • Jiang, S.1    Meyer, R.2    Kang, K.3    Osborne, C.K.4    Wong, J.5    Oesterreich, S.6
  • 23
    • 33846336842 scopus 로고    scopus 로고
    • Multiple repressor pathways contribute to phenotypic switching of vascular smooth muscle cells
    • Kawai-Kowase K, Owens GK. 2007. Multiple repressor pathways contribute to phenotypic switching of vascular smooth muscle cells. Am J Physiol Cell Physiol 292: C59-C69.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Kawai-Kowase, K.1    Owens, G.K.2
  • 24
    • 33846928412 scopus 로고    scopus 로고
    • Specific amino acid residues in the bHLH domain of SRC-3 are essential for its nuclear localization and proteasome-dependant turnover
    • Li C, Wu RC, Amazit L, Tsai SY, Tsai MJ, O'Malley BW. 2006. Specific amino acid residues in the bHLH domain of SRC-3 are essential for its nuclear localization and proteasome-dependant turnover. Mol Cell Biol 27:1296-1308.
    • (2006) Mol Cell Biol , vol.27 , pp. 1296-1308
    • Li, C.1    Wu, R.C.2    Amazit, L.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 25
    • 0032489555 scopus 로고    scopus 로고
    • The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation
    • Li H, Chen JD. 1998. The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation. J Biol Chem 273: 5948-5954.
    • (1998) J Biol Chem , vol.273 , pp. 5948-5954
    • Li, H.1    Chen, J.D.2
  • 26
    • 0030872716 scopus 로고    scopus 로고
    • RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2
    • Li H, Gomes PJ, Chen JD. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc Natl Acad Sci USA 94:8479-8484.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8479-8484
    • Li, H.1    Gomes, P.J.2    Chen, J.D.3
  • 27
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li H, Leo C, Zhu J, Wu X, O'Neil J, Park EJ, Chen JD. 2000. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol 20:1784-1796.
    • (2000) Mol Cell Biol , vol.20 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.J.6    Chen, J.D.7
  • 28
    • 33646133406 scopus 로고    scopus 로고
    • The expanding cosmos of nuclear receptor coactivators
    • Lonard DM, O'Malley BW. 2006. The expanding cosmos of nuclear receptor coactivators. Cell 125:411-414.
    • (2006) Cell , vol.125 , pp. 411-414
    • Lonard, D.M.1    O'Malley, B.W.2
  • 30
    • 0033842610 scopus 로고    scopus 로고
    • Prothymosin alpha selectively enhances estrogen receptor transcriptional activity by interacting with a repressor of estrogen receptor activity
    • Martini PG, Delage-Mourroux R, Kraichely DM, Katzenellenbogen BS. 2000. Prothymosin alpha selectively enhances estrogen receptor transcriptional activity by interacting with a repressor of estrogen receptor activity. Mol Cell Biol 20:6224-6232.
    • (2000) Mol Cell Biol , vol.20 , pp. 6224-6232
    • Martini, P.G.1    Delage-Mourroux, R.2    Kraichely, D.M.3    Katzenellenbogen, B.S.4
  • 31
    • 0028874666 scopus 로고
    • The tissue-specific nuclear matrix protein, NMP-2, is a member of the AML/CBF/PEBP2/runt domain transcription factor family: Interactions with the osteocalcin gene promoter
    • Merriman HL, van Wijnen AJ, Hiebert S, Bidwell JP, Fey E, Lian J, Stein J, Stein GS. 1995. The tissue-specific nuclear matrix protein, NMP-2, is a member of the AML/CBF/PEBP2/runt domain transcription factor family: Interactions with the osteocalcin gene promoter. Biochemistry 34:13125-13132.
    • (1995) Biochemistry , vol.34 , pp. 13125-13132
    • Merriman, H.L.1    van Wijnen, A.J.2    Hiebert, S.3    Bidwell, J.P.4    Fey, E.5    Lian, J.6    Stein, J.7    Stein, G.S.8
  • 32
    • 0033536054 scopus 로고    scopus 로고
    • An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens
    • Montano MM, Ekena K, Delage-Mourroux R, Chang W, Martini P, Katzenellenbogen BS. 1999. An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens. Proc Natl Acad Sci USA 96:6947-6952.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6947-6952
    • Montano, M.M.1    Ekena, K.2    Delage-Mourroux, R.3    Chang, W.4    Martini, P.5    Katzenellenbogen, B.S.6
  • 33
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M, Tansey WP. 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
  • 36
    • 0242443220 scopus 로고    scopus 로고
    • Scaffold attachment factors SAFB1 and SAF B2: Innocent bystanders or critical players in breast tumorigenesis?
    • Oesterreich S. 2003. Scaffold attachment factors SAFB1 and SAF B2: Innocent bystanders or critical players in breast tumorigenesis? J Cell Biochem 90:653-661.
    • (2003) J Cell Biochem , vol.90 , pp. 653-661
    • Oesterreich, S.1
  • 37
    • 0034463079 scopus 로고    scopus 로고
    • Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation
    • Oesterreich S, Zhang Q, Hopp T, Fuqua SA, Michaelis M, Zhao HH, Davie JR, Osborne CK, Lee AV. 2000. Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation. Mol Endocrinol 14:369-381.
    • (2000) Mol Endocrinol , vol.14 , pp. 369-381
    • Oesterreich, S.1    Zhang, Q.2    Hopp, T.3    Fuqua, S.A.4    Michaelis, M.5    Zhao, H.H.6    Davie, J.R.7    Osborne, C.K.8    Lee, A.V.9
  • 38
    • 0033616676 scopus 로고    scopus 로고
    • SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor
    • Park EJ, Schroen DJ, Yang M, Li H, Li L, Chen JD. 1999. SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor. Proc Natl Acad Sci USA 96:3519-3524.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3519-3524
    • Park, E.J.1    Schroen, D.J.2    Yang, M.3    Li, H.4    Li, L.5    Chen, J.D.6
  • 39
    • 2342573009 scopus 로고    scopus 로고
    • The role of corepressors in transcriptional regulation by nuclear hormone receptors
    • Privalsky ML. 2004. The role of corepressors in transcriptional regulation by nuclear hormone receptors. Annu Rev Physiol 66:315-360.
    • (2004) Annu Rev Physiol , vol.66 , pp. 315-360
    • Privalsky, M.L.1
  • 40
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y, Hu X, DiRenzo J, Lazar MA, Brown M. 2000. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103:843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 41
    • 4143093854 scopus 로고    scopus 로고
    • Coactivator AIB1 links estrogen receptor transcriptional activity and stability
    • Shao W, Keeton EK, McDonnell DP, Brown M. 2004. Coactivator AIB1 links estrogen receptor transcriptional activity and stability. Proc Natl Acad Sci USA 101:11599-11604.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11599-11604
    • Shao, W.1    Keeton, E.K.2    McDonnell, D.P.3    Brown, M.4
  • 42
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 43
    • 0034213318 scopus 로고    scopus 로고
    • Expresssion of a repressor of estrogen receptor activity in human breast tumors: Relationship to some known prognostic markers
    • Simon SL, Parkes A, Leygue E, Dotzlaw H, Snell L, Troup S, Adeyinka A, Watson PH, Murphy LC. 2000. Expresssion of a repressor of estrogen receptor activity in human breast tumors: Relationship to some known prognostic markers. Cancer Res 60:2796-2799.
    • (2000) Cancer Res , vol.60 , pp. 2796-2799
    • Simon, S.L.1    Parkes, A.2    Leygue, E.3    Dotzlaw, H.4    Snell, L.5    Troup, S.6    Adeyinka, A.7    Watson, P.H.8    Murphy, L.C.9
  • 44
    • 0034655187 scopus 로고    scopus 로고
    • Nuclear structure-gene expression interrelationships: Implications for aberrant gene expression in cancer
    • Stein GS, Montecino M, van Wijnen AJ, Stein JL, Lian JB. 2000. Nuclear structure-gene expression interrelationships: Implications for aberrant gene expression in cancer. Cancer Res 60:2067-2076.
    • (2000) Cancer Res , vol.60 , pp. 2067-2076
    • Stein, G.S.1    Montecino, M.2    van Wijnen, A.J.3    Stein, J.L.4    Lian, J.B.5
  • 46
    • 2942711582 scopus 로고    scopus 로고
    • Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor- B1: Identification of a potent transcriptional repression domain
    • Townson SM, Kang K, Lee AV, Oesterreich S. 2004. Structure-function analysis of the estrogen receptor alpha corepressor scaffold attachment factor- B1: Identification of a potent transcriptional repression domain. J Biol Chem 279:26074-26081.
    • (2004) J Biol Chem , vol.279 , pp. 26074-26081
    • Townson, S.M.1    Kang, K.2    Lee, A.V.3    Oesterreich, S.4
  • 48
    • 0025812291 scopus 로고
    • Direct repeats as selective response elements for the thyroid hormone induced gene expression through a common responsive element
    • Umesono K, Murakami KK, Thompson CC, Evans RM. 1991. Direct repeats as selective response elements for the thyroid hormone induced gene expression through a common responsive element. Cell 65:1255-1266.
    • (1991) Cell , vol.65 , pp. 1255-1266
    • Umesono, K.1    Murakami, K.K.2    Thompson, C.C.3    Evans, R.M.4
  • 49
    • 0035844255 scopus 로고    scopus 로고
    • Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of R IP140
    • Wei LN, Farooqui M, Hu X. 2001. Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of R IP140. J Biol Chem 276:16107-16112.
    • (2001) J Biol Chem , vol.276 , pp. 16107-16112
    • Wei, L.N.1    Farooqui, M.2    Hu, X.3
  • 50
    • 0034731401 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing
    • Wei LN, Hu X, Chandra D, Seto E, Farooqui M. 2000. Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J Biol Chem 275:40782-40787.
    • (2000) J Biol Chem , vol.275 , pp. 40782-40787
    • Wei, L.N.1    Hu, X.2    Chandra, D.3    Seto, E.4    Farooqui, M.5
  • 51
    • 0037732643 scopus 로고    scopus 로고
    • Active repression by unliganded retinoid receptors in development: Less is sometimes more
    • Weston AD, Blumberg B, Underhill TM. 2003. Active repression by unliganded retinoid receptors in development: Less is sometimes more. J Cell Biol 161:223-228.
    • (2003) J Cell Biol , vol.161 , pp. 223-228
    • Weston, A.D.1    Blumberg, B.2    Underhill, T.M.3
  • 53
    • 0033454007 scopus 로고    scopus 로고
    • The nuclear-receptor interacting protein (RIP) 140 binds to the human glucocorticoid receptor and modulates hormone-dependent transactivation
    • Windahl SH, Treuter E, Ford J, Zilliacus J, Gustafsson JA, McEwan IJ. 1999, The nuclear-receptor interacting protein (RIP) 140 binds to the human glucocorticoid receptor and modulates hormone-dependent transactivation. J Steroid Biochem Mol Biol 71:93-102.
    • (1999) J Steroid Biochem Mol Biol , vol.71 , pp. 93-102
    • Windahl, S.H.1    Treuter, E.2    Ford, J.3    Zilliacus, J.4    Gustafsson, J.A.5    McEwan, I.J.6
  • 54
    • 18844373937 scopus 로고    scopus 로고
    • Transcriptional regulation by steroid receptor coactivator phosphorylation
    • Wu RC, Smith CL, O'Malley BW. 2005. Transcriptional regulation by steroid receptor coactivator phosphorylation. Endocr Rev 26:393-399.
    • (2005) Endocr Rev , vol.26 , pp. 393-399
    • Wu, R.C.1    Smith, C.L.2    O'Malley, B.W.3
  • 55
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu L, Glass CK, Rosenfeld MG. 1999. Coactivator and corepressor complexes in nuclear receptor function. Curr Opin Genet Dev 9:140-147.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 56
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition
    • Zhou BP, Deng J, Xia W, Xu J, Li YM, Gunduz M, Hung MC. 2004. Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat Cell Biol 6:931-940.
    • (2004) Nat Cell Biol , vol.6 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6    Hung, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.